Epitope prediction based on random peptide library screening has become a focus as a promising method in immunoinformatics research. Some novel software and web-based servers have been proposed in recent years and have succeeded in given test cases. However, since the number of available mimotopes with the relevant structure of template-target complex is limited, a systematic evaluation of these methods is still absent. In this study, a new benchmark dataset was defined. Using this benchmark dataset and a representative dataset, five examples of the most popular epitope prediction software products which are based on random peptide library screening have been evaluated. Using the benchmark dataset, in no method did performance exceed a 0.42 precision and 0.37 sensitivity, and the MCC scores suggest that the epitope prediction results of these software programs are greater than random prediction about 0.09-0.13; while using the representative dataset, most of the values of these performance measures are
Based on years of experience in phage display technology, Creative Biolabs now is able to provide services for the construction and screening of immune antibody library.. With years of research and development in the past decades, phage display has been a powerful technology to display millions or even billions of different peptides or proteins. It is now a common choice for the studies of protein-protein, protein-peptide and protein-DNA interactions. Among all the applications of phage display technology, one of the most successful ones is the isolation of monoclonal antibodies utilizing large capacity phage antibody libraries.. Thanks to the rapid development of this technology, it has become a reliable tool for the production of monoclonal antibody with high specificity and affinity. "Compared with conventional hybridoma technology, the generation of immune antibody libraries is not limited by the requirement of fusion partners. This expands the possibility to develop monoclonal antibodies ...
Having been researching in the field of phage display technology for years, Creative Biolabs is able to offer a series of comprehensive phage display library screening services by its own biopanning strategies and enhanced equipments.. Phage display technology is one of the major approaches applied in various protein interaction studies, especially in the discovery of specific antibodies, scaffolds and ligands. As binders with the desired specificity generally exist at low frequencies in the constructed libraries, phage display library screening has become an effective technique for the enrichment and identification of binders with high affinity and specificity from interested libraries.. Libraries from customized library construction services, in-house premade antibody libraries, peptide libraries or scaffold libraries, libraries provided by clients and other commercialized libraries can all be screened in Creative Biolabs.. "No matter its purified or unpurified targets, we can screen for ...
This paper reports the synthesis and screening of a combinatorial peptide library for new affinity ligands for glycosylated haemoglobin (HbA(1c)), which is an important indicator of diabetes control. The new ligands are suitable for large-scale synthesis and overcome the disadvantages of antibodies (unstable and expensive to produce etc.), while remaining as efficient as antibodies in binding to the analyte. The library consisted of 262 144 hexapeptides synthesised using the one-bead-one-compound technique. The hexapeptides attached onto beads were screened with glycosylated haemoglobin HbA(1c). The structures of the peptides exhibiting high affinity were characterised by Edman microsequencing. Computer modelling simulation of one of the lead sequences has shown that this class of ligand has a high affinity and specificity for glycosylated haemoglobin. (C) 1998 Elsevier Science S.A. All rights reserved.. ...
Since the advent of phage display technology, dating back to 1985, antibody libraries displayed on filamentous phage surfaces have been used to identify specific binders for many different purposes, including the recognition of tumors. Phage display represents a high-throughput technique for screening billions of random fusion antibodies against virtually any target on the surface or inside cancer cells, or even soluble markers found in patient serum. Many phage display derived binders targeting important tumor markers have been identified. Selection directed to tumoral cells surfaces lead to the identification of unknown tumoral markers. Also the improvement of methods that require smaller amounts of cells has opened the possibility to use this approach on patient samples. Robust techniques combining an antibody library displayed on the phage surface and protein microarray allowed the identification of auto antibodies recognized by patient sera. Many Ab molecules directly or indirectly targeting
0054]Other methods, such as preparation of random peptide libraries or epitope libraries are well known in the art and may be used to reproducibly produce antigens. E.g., J. K. Scott & G. P. Smith, Searching for Peptide Ligands with an Epitope Library, 249 Science 386 (1990); J. J. Devlin et al., Random Peptide Libraries: A Source of Specific Protein Binding Molecules, 249 Science 404-406 (1990); S. E. Cwirla et al., Peptides on Phage: A Vast Library of Peptides for Identifying Ligands, 87 Proc. Natl Acad. Sci. USA 6378-6382 (1990); K. S. Lam et al., A New Type of Synthetic Peptide Library for Identifying Ligand-binding Activity, 354 Nature 82-84 (1991); S. Cabilly, Combinatorial Peptide Library Protocols (Humana Press, 304 pp, 1997); U.S. Pat. No. 5,885,780. Such libraries may be constructed by ligating synthetic oligonucleotides into an appropriate fusion phage. Fusion phages are filamentous bacteriophage vectors in which foreign sequences are cloned into phage gene III and displayed as part ...
TY - JOUR. T1 - Peptide mimotopes of oncoproteins as therapeutic agents in breast cancer.. AU - Ashok, B. T.. AU - David, L.. AU - Chen, Y. G.. AU - Garikapaty, V. P.. AU - Chander, B.. AU - Kanduc, D.. AU - Mittelman, A.. AU - Tiwari, R. K.. PY - 2003/4. Y1 - 2003/4. N2 - Generation of an immune response to oncoproteins can lead to a cancer specific protective immunity. Several such oncoproteins are being examined as tumor targets with mixed results. We are evaluating the clinical utility of synthetic peptides that would mimic the antigen immunologically and elicit a tumor specific immune response. HER-2/neu, an oncoprotein whose expression in breast cancer is associated with poor prognosis, lower disease free-survival and a propensity for metastases was chosen as a model. Antibodies, Ab2, Ab4 and Ab5 directed towards the extracellular domain of HER-2/neu were reacted to peptides from two synthetic phage display peptide libraries, LX-8 (12-mer peptide library containing disulfide bridge) and ...
Rx Biosciences offers construction and screening of custom bacterial display libraries of small peptides. The library is useful in ligand discovery, antibody-antigen binding affinity study and identification of targets. Libraries of polypeptides displayed on the surface of bacteria are screened using flow cytometry or routinely used selection procedures (biopanning). The library is created by combining a highly diverse collection of synthetically-constructed randomized peptide sequences using a unique proprietary technique. The library has been specifically optimized to eliminate unwanted stop codons and aggregation-prone sequences. As in a phage display, the peptides the bacterial display peptides are expressed at the surface (plasma membrane) as a conjugated protein. The expression of the peptides is inducible.. We accept customer supplied vectors also and the customer owns the exclusive rights.. ...
628 Nasopharyngeal carcinoma (NPC) is one of the most common cancers among Chinese living in South China, Taiwan and Singapore. For treatment of NPC, although radiotherapy, surgical removal, and chemotherapy have been applied for decades and the 5 year survival rate in the advanced cases are still below 75 %. Much effort using other methods such as high dose chemotherapy plus bone marrow stem cell injection and other targeting therapy are needed to control this cancer. In the present experiment, we used random peptide phage display libraries to identify and isolate a specific novel peptide from NPC cell line for targeting drug delivery. After subtraction with control epithelial cells for 3 times, the remained phage libraries were biopanning on NPC-TW04 cells for 5 rounds. It was found that 44 selected phage clones could specifically bind to NPC cell surface. When ELISA was used to verify those clones, 16 phage clones showed higher affinity to NPC cells and were subjected to DNA sequencing. The ...
TY - JOUR. T1 - Automated panning and screening procedure on microplates for antibody generation from phage display libraries. AU - Turunen, Laura. AU - Takkinen, Kristiina. AU - Söderlund, Hans. AU - Pulli, Timo. PY - 2009. Y1 - 2009. N2 - Antibody phage display technology is well established and widely used for selecting specific antibodies against desired targets. Using conventional manual methods, it is laborious to perform multiple selections with different antigens simultaneously. Furthermore, manual screening of the positive clones requires much effort. The authors describe optimized and automated procedures of these processes using a magnetic bead processor for the selection and a robotic station for the screening step. Both steps are performed in a 96-well microplate format. In addition, adopting the antibody phage display technology to automated platform polyethylene glycol precipitation of the enriched phage pool was unnecessary. For screening, an enzyme-linked immunosorbent assay ...
We plan to do some fishing into a random peptide library and would like to know the experience of those that have used constrained peptides vs unconstrained peptides. Are peptides that are removed from their constrained vectors likely to still function in an unconstrained context? ie is the greater likelyhood of getting a hit on the constrained library offset by the potential lack of function when the peptides are subsequently used unconstrained? -- Scott Vande Pol Case Western Reserve University Department of Pathology Cleveland Oh. 44106 sbv at pop.cwru.edu ...
A peptide library is a tool for protein-related study. A peptide library contains a great number of peptides that have a systematic combination of amino acids. Usually, peptide library is synthesized on solid phase, mostly on resin, which can be made as flat surface or beads. The peptide library provides a powerful tool for drug design, protein-protein interactions, and other biochemical as well as pharmaceutical applications. You can create a mix of desired amino acids at each point in a sequence. In this way, you could create a library of 20 different polypeptides with only one amino acid residue at random and the rest being the same. The usefulness of this form of peptide synthesis is limited as you cant go beyond 70 acids in length. This would give you 2070 possible combinations and thats only if you dont include the plethora of available amino acids with pre-installed post-translational modifications. Most drug development does not involve such a random assortment of proteins as you ...
... , protein peptide and polypeptide smallest to largest fraction, piruvato quinase glucagon like peptide, genscript custom peptide, nitrobenzyl cysteine peptide, hexahistidine peptide calculator, lupuzor peptide 1402, is erythropoietin a peptide hormone, antigenic peptide prediction bioinformatics tools blast, kinerase pro therapy c8 peptide intensive face treatment reviews, tat peptide sequence calculator, superdex peptide 10 300 gl column wraps, peptide antigen processing pathway, over the counter medications to treat anxiety, the proceedings of 20th american peptide symposium, antigenic peptide prediction server products, gap 27 peptide calculator, what stomach enzyme breaks down peptide bonds, igf 1 peptide therapy
The interaction between a CD4+ TH cell and an antigen presenting cell (APC) is a finely tuned event in adaptive immunity. The affinity is dictated by the T cell receptor (TCR) and the characteristics of antigenic peptide epitopes presented on the major histocompatibility complex class II (pMHC class II) molecules on APCs. Due to the high degree of polymorphism in MHC molecules and the vast repertoire of epitopes that may be presented on each, it is an immense challenge to predict epitopes relevant to disease and homeostasis. It would therefore be of very high value to develop a technology that allows for precise experimental identification of T cell epitopes in the absence of any prior knowledge of the relevant antigen, as long as one has access to T cells. We have developed a novel and generic combinatorial display system for MHC class II, based on phage display. Using phage display, one can probe an epitope sequence space orders of magnitude larger than any cellular or chemical system. As a ...
article{c02feb63-0c75-498d-9b63-6043d6df0ab2, abstract = {Background: Phage Display technology is a well established technique for high throughput screening of affinity ligands. Here we describe a new compact chromato-panning procedure for selection of suitable binders from a phage peptide display library. Results: Both phages and E. coli cells pass non-hindered through the interconnected pores of macroporous gel, so called cryogel. After coupling a ligand to a monolithic cryogel column, the phage library was applied on the column and non-bound phages were washed out. The selection of strong phage-binders was achieved already after the first panning cycle due to the efficient separation of phage-binders from phage-non-binders in chromatographic mode rather than in batch mode as in traditional biopanning procedures. E. coli cells were applied on the column for infection with the specifically bound phages. Conclusion: Chromato-panning allows combining several steps of the panning procedure ...
With the success of the human genome project, the focus of life science research has shifted to the functional and structural analyses of proteins, such as the fields of proteomics and structural genomics. These analyses of proteins, including newly identified proteins, are expected to contribute to the identification of therapeutically applicable proteins for various diseases. Thus, pharmacoproteomic-based drug discovery and the development of protein therapies has currently attracted a great deal of attention (1, 2, 3) . However, it is clinically difficult to use most bioactive proteins, such as tumor necrosis factor-α (TNF-α), as antitumor agents because of their very low stability and pleiotropic action in vivo (4 , 5) .. TNF-α was reported to exert a strong cytotoxicity to various kinds of tumor cells but not to normal cells in vitro and to cause hemorrhagic necrosis of certain transplanted solid tumors (6) . Thus, TNF-α has been considered a promising new drug for cancer therapy. On ...
The product of the HER2/Neu oncogene is a receptor tyrosine kinase that is amplified in 25-30% of human primary breast tumors. In this project? we have isolated the HER2/Neu kinase from Sf9 cells infected with a baculovirus expression vector. We probed the substrate specificity of the HER2/Neu kinase using two peptide libraries: (1) a soluble peptide library containing three degenerate positions N-terminal to tyrosine; and (2) a bead-supported combinatorial library possessing sis degenerate positions at P - 1, P - 2, P - 3, P + 1, P + 2, and P + 3. We identified four novel substrate sequences for HER2/Neu from the two peptide libraries. We synthesized these peptides as individual sequences and measured steady-state kinetic properties for phosphorylation by HER2/Neu. One of the peptides, AAEEIYAARRG, is the best synthetic peptide substrate reported to date for HER2/Neu. All of the sequences bear a resemblance to sites of autophosphorylation on HER2/Neu and related epidermal growth factor (EGF) ...
Directed evolution is a powerful method for engineering of specific affinity proteins such as antibodies and alternative scaffold proteins. For selections from combinatorial protein libraries, robust and high-throughput selection platforms are needed. An attractive technology for this purpose is cell surface display, offering many advantages, such as the quantitative isolation of high-affinity library members using flow-cytometric cell sorting. This thesis describes the development, evaluation and use of bacterial display technologies for the engineering of affinity proteins.. Affinity proteins used in therapeutic and diagnostic applications commonly aim to specifically bind to disease-related drug targets. Angiogenesis, the formation of new blood vessels from pre-existing vasculature, is a critical process in various types of cancer and vascular eye disorders. Vascular Growth Factor Receptor 2 (VEGFR2) is one of the main regulators of angiogenesis. The first two studies presented in this thesis ...
Directed evolution is a powerful method for engineering of specific affinity proteins such as antibodies and alternative scaffold proteins. For selections from combinatorial protein libraries, robust and high-throughput selection platforms are needed. An attractive technology for this purpose is cell surface display, offering many advantages, such as the quantitative isolation of high-affinity library members using flow-cytometric cell sorting. This thesis describes the development, evaluation and use of bacterial display technologies for the engineering of affinity proteins. Affinity proteins used in therapeutic and diagnostic applications commonly aim to specifically bind to disease-related drug targets. Angiogenesis, the formation of new blood vessels from pre-existing vasculature, is a critical process in various types of cancer and vascular eye disorders. Vascular Growth Factor Receptor 2 (VEGFR2) is one of the main regulators of angiogenesis. The first two studies presented in this thesis ...
LifeTein Peptide Library: SARS-CoV-2 Receptor Binding Domain, 4 Fragments [LT-V013] - Overlapping Peptide Library: The SARS-CoV-2 Receptor Binding Domain is divided in to 4 fragments of 20 amino acids per peptide. The resulting overlapping peptide libraries can then be used for processes including continuous and linear epitope mapping, antibody screening and characterization. Reference 1: A highly conserved cryptic epitope in the receptor-binding
Heparan sulfate (HS) binds and modulates the transport and activity of a large repertoire of regulatory proteins. The HS phage display antibodies are powerful tools for the analysis of native HS structure in situ; however, their epitopes are not well defined. Analysis of the binding specificities of a set of HS antibodies by competitive binding assays with well defined chemically modified heparins demonstrates that O-sulfates are essential for binding; however, increasing sulfation does not necessarily correlate with increased antibody reactivity. IC50 values for competition with double modified heparins were not predictable from IC50 values with corresponding singly modified heparins. Binding assays and immunohistochemistry revealed that individual antibodies recognize distinct epitopes and that these are not single linear sequences but families of structurally similar motifs in which subtle variations in sulfation and conformation modify the affinity of interaction. Modeling of the antibodies ...
Principal Investigator:ITOH Kunihiko, Project Period (FY):1996 - 1997, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:応用薬理学・医療系薬学
Reconstitution of a neocytokine from the first 30 aa of IL-2 is very novel in the field of peptide agonists. Recently characterized peptides, with agonist activities related to cytokines of the hemopoietin family, have consisted up to this point of small mimetics of erythropoietin (EPO (28)) or thrombopoietin (29) selected by random phage display peptide libraries and a small nonpeptidyl mimic of G-CSF (30). These compounds act as full agonists in various biological assays, and their signaling pathways appear to be identical to those induced by the natural ligand, yet their amino acid sequences are not found in the primary sequence of the natural protein. The crystal structure of the 20-aa mimetic peptide of EPO and of the extracellular domain of the EPO receptor (EPOR) reveals a dimerization of the peptide that is bound to the homodimeric EPOR. In this study, it was shown that the peptide p1-30 contains a part of the native aa sequence of IL-2, forms a tetrameric structure that mimics a ...
Phage display is a method to discover peptide ligands while minimizing and optimizing the structure and function of proteins (Hallahan, 2003). The phage is used as a scaffold to display recombinant libraries of peptides and provides a means to recover and amplify the peptides that bind to putative receptor molecules in vivo. In vivo selection simultaneously provides positive and subtractive screens because organs and tissues such as tumors are spatially separated. Phage DNA can then be sequenced to determine the amino acid sequence of peptides on the capsid that have been recovered from tumors. The T7 phage display system exploits the T7 capsid protein as a scaffold to display peptides on the capsid protein unique to the 10B protein on the surface of the phage. Gene 10 encoding the capsid protein is cloned with a series of multiple cloning sites at the C-terminus of the 10B protein. The natural translational frame shift site within the capsid gene has been removed so that only a single form of ...
The aim of this work was to verify the possibility of applying affinity chromatography in bacteriophage purification, from the perspective of therapeutic purposes. Elution profiles of phages modified with specific affinity motifs (Figures 3,4,5 and 6) show substantially higher phage concentration in elution fractions compared to final washing samples. This indicates binding of modified phages to the affinity resins and effective elution with standard competitive agents. Thus, affinity tags can be successfully incorporated into the T4 phage capsid by the in vivo phage display technique and they strongly elevate bacteriophage affinity to a specific resin. Non-specific binding was also observed: unmodified phages or those modified with the non-specific tag were eluted with the titre 104-105 pfu/ml. Nevertheless, the unspecific binding is 102-105 times weaker than the specific one and importantly it does not interfere with the aim of preparation of purified anti-bacterial active bacteriophages for ...
We are leaders in the field of human antibody engineering and have been involved in many of the seminal discoveries in the field. We are experts in phage, yeast and lentivirus display platforms and panning procedures, human antibody library constructions, Fc engineering, humanization procedures and targeted siRNA delivery to name a few. We have constructed human antibody libraries with tens of billion members and have successfully isolated therapeutic human antibodies against over two dozen targets. We have also developed and utilize antibody expression systems in bacteria, mammalian, yeast and insect cells. Students and post-doctoral fellows join the Marasco lab to become skilled artisans in the field under Dr. Marascos mentorship. An overview of some of our antibody engineering tools can be found here. ...
Close The Infona portal uses cookies, i.e. strings of text saved by a browser on the users device. The portal can access those files and use them to remember the users data, such as their chosen settings (screen view, interface language, etc.), or their login data. By using the Infona portal the user accepts automatic saving and using this information for portal operation purposes. More information on the subject can be found in the Privacy Policy and Terms of Service. By closing this window the user confirms that they have read the information on cookie usage, and they accept the privacy policy and the way cookies are used by the portal. You can change the cookie settings in your browser. ...
Abstract. Currently, novel drug design focused on the searching pharmacological compounds acting via influence on GPCRs heteromers. The strategy allows obtaining highly selective effects since these heteromers appear only on specific cells and tissues. Therefore, human monoclonal scFv antibodies able to recognizing GPCRs heteromers may constitute a valuable tool in modern therapies. Antibody phage display technique together with high throughput screening play a key role in the development of clinically useful immunomolecules. Therefore in the present work we focused on the comparison of various strategies used for biopanning process during phage display procedure, dedicated to isolation scFv antibodies specifically recognizing GPCRs heteromers. Experiments were conducted in two different cell lines (CHO-K1 and HEK 293) and six various selection procedures were described. Elimination of nonspecific bindings constitutes a key point during the process. Results obtained duing selection conducted in ...
Adamalysin-like metalloproteinases with thrombospondin (TS) motifs (ADAMTS)-5 is the multi-domain metalloproteinase that most potently degrades aggrecan proteoglycan in the cartilage and its activity is implicated in the development of osteoarthritis (OA). To generate specific exosite inhibitors for it, we screened a phage display antibody library in the presence of the zinc-chelating active site-directed inhibitor GM6001 (Ilomastat) and isolated four highly selective inhibitory antibodies. Two antibodies were mapped to react with exosites in the catalytic/disintegrin domains (Cat/Dis) of the enzyme, one in the TS domain and one in the spacer domain (Sp). The antibody reacting with the Sp blocked the enzyme action only when aggrecan or the Escherichia coli-expressed aggrecan core protein were substrates, but not against a peptide substrate. The study with this antibody revealed the importance of the Sp for effective aggrecanolytic activity of ADAMTS-5 and that this domain does not interact with sulfated
In vivo screening of phage-displayed peptide libraries has revealed extensive molecular differences in the blood vessels of individual normal tissues. Pathological lesions also put their signature on the vasculature; in tumours, both blood and lymphatic vessels differ from normal vessels. The changes that characterize tumour blood vessels include selective expression of certain integrins. Peptides isolated by in vivo phage display for homing to tumours have been shown to be useful in directing therapeutic agents to experimental tumours. The targeting can enhance the efficacy of the therapy while reducing side effects. Phage screening has also revealed lung-specific vascular markers that promote tumour metastasis to the lungs by mediating specific adherence of tumour cells to the lung vasculature. These phage-screening studies have revealed a previously unsuspected degree of vascular specialization and provide potentially useful guidance devices for targeted therapies.. ...
The display of repertoires of antibody fragments on the surface of filamentous phage offers a new way to produce immunoreagents with defined specificities. Phage derived antibody fragments offer a number of advantages over mouse monoclonal antibodies, such as better clearance from the blood, the possibility to select from human combinatorial libraries and the relative ease by which such fragments can be manipulated. The phage display technique thus facilitates the selection of antibody fragments of therapeutic value or research interest. Antibodies to M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface ...
The display of repertoires of antibody fragments on the surface of filamentous phage offers a new way to produce immunoreagents with defined specificities. Phage derived antibody fragments offer a number of advantages over mouse monoclonal antibodies, such as better clearance from the blood, the possibility to select from human combinatorial libraries and the relative ease by which such fragments can be manipulated. The phage display technique thus facilitates the selection of antibody fragments of therapeutic value or research interest. Antibodies to M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface ...
Several applications in the area of drug design and drug delivery utilize peptide libraries. Select a link on our interactive display for descriptions and publications for the highlighted peptide library applications.
Abstract:. MHC class I molecules (HLA-I in humans) present peptides derived from endogenous proteins to CTLs. Whereas the peptide-binding specificities of HLA-A and -B molecules have been studied extensively, little is known about HLA-C specificities. Combining a positional scanning combinatorial peptide library approach with a peptide-HLA-I dissociation assay, in this study we present a general strategy to determine the peptide-binding specificity of any MHC class I molecule. We applied this novel strategy to 17 of the most common HLA-C molecules, and for 16 of these we successfully generated matrices representing their peptide-binding motifs. The motifs prominently shared a conserved C-terminal primary anchor with hydrophobic amino acid residues, as well as one or more diverse primary and auxiliary anchors at P1, P2, P3, and/or P7. Matrices were used to generate a large panel of HLA-C-specific peptide-binding data and update our pan-specific NetMHCpan predictor, whose predictive performance ...
Since the development of antibody-production techniques, a number of immunoglobulins have been developed on a large scale using conventional methods. Hybridoma technology opened a new horizon in the production of antibodies against target antigens of infectious pathogens, malignant diseases including autoimmune disorders, and numerous potent toxins. However, these clinical humanized or chimeric murine antibodies have several limitations and complexities. Therefore, to overcome these difficulties, recent advances in genetic engineering techniques and phage display technique have allowed the production of highly specific recombinant antibodies. These engineered antibodies have been constructed in the hunt for novel therapeutic drugs equipped with enhanced immunoprotective abilities, such as engaging immune effector functions, effective development of fusion proteins, efficient tumor and tissue penetration, and high-affinity antibodies directed against conserved targets. Advanced antibody engineering
Phage display technology for identifying selective antigens and address molecules on brain endothelial cells. In Blood Barrier: Biology and Research Protocols (Ed. S. Nag)
A phage display library was used to identify peptide sequences that target bone. The objective was to investigate the effect of these...
Video articles in JoVE about natriuretic peptides include High Efficiency Differentiation of Human Pluripotent Stem Cells to Cardiomyocytes and Characterization by Flow Cytometry, Methods for the Isolation, Culture, and Functional Characterization of Sinoatrial Node Myocytes from Adult Mice, Assessing Endothelial Vasodilator Function with the Endo-PAT 2000, Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates, Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation, Distinguishing Allosteric Effects from Orthosteric Binding in Protein-Ligand Interactions, Technique of Minimally Invasive Transverse Aortic Constriction in Mice for Induction of Left Ventricular Hypertrophy, Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies, Microwave-assisted Functionalization
JPT Peptide Technologies is a DIN ISO 9001:2015 certified and GCLP compliant integrated provider of innovative peptide based catalog products and custom services.
Description of Phage Display (from New England Biolabs). Phage display describes a selection technique in which a peptide or protein is expressed as a fusion with a coat protein of a bacteriophage, resulting in display of the fused protein on the exterior surface of the phage virion, while the DNA encoding the fusion resides within the virion. Phage display has been used to create a physical linkage between a vast library of random peptide sequences to the DNA encoding each sequence, allowing rapid identification of peptide ligands for a variety of target molecules (antibodies, enzymes, cell-surface receptors, etc.) by an in vitro selection process called biopanning.. In its simplest form, biopanning is carried out by incubating a library of phage-displayed peptides with a plate (or bead) coated with the target, washing away the unbound phage, and eluting the specifically-bound phage. (Alternatively the phage can be reacted with the target in solution, followed by affinity capture of the ...
Bacterial display or bacterial surface display is a commonly used protein engineering technique, especially in terms of in vitro protein evolution. Libraries of polypeptides displayed on the surface of bacteria can be screened using flow cytometry or iterative selection procedures. This protein engineering technique allows us to put together the function of a protein and the gene that encodes it. Bacterial display can be used to find target proteins with desired properties and can be used to make affinity ligands which are cell-specific. This system can be used in many applications including the creation of novel vaccines, the identification of enzyme substrates and finding the affinity of a ligand for its target protein. ...
Peptide libraries can be screened to identify important binding epitopes to develop effective vaccines against many viral diseases.
T-cell Truncated peptide libraries allow the testing of all possible T-cell epitopes (ie. all 8 to 11-mers) across a protein of interest.
SCREEN-WELL(R) Cholinergic ligand library(500 ul/well) https://www.sciencepro.com.br/produtos/bml-2815-0500 https://www.sciencepro.com.br/@@site-logo/logo-novo.png ...
SCREEN-WELL(R) Histaminergic ligand library(100 ul/well) https://www.sciencepro.com.br/produtos/bml-2816-0100 https://www.sciencepro.com.br/@@site-logo/logo-novo.png ...
LinkedIn: Chinese Hamster Ovary cells, known as CHO, play an important role in modern medicine. NISTs new CHO peptide library will enable better production of treatments for psoriasis, cancer, hemophilia and leukemia.
miR-6883 Family miRNAs Target CDK4/6 to Induce G1 Phase Cell Cycle Arrest in Colon Cancer Cells Ectopic expression of miR-6883-5p or miR-149* downregulated CDK4 and CDK6 levels in human colorectal cancer cells. [Cancer Res] Abstract USP7 Is a Tumor-Specific WNT Activator for APC-Mutated Colorectal Cancer by Mediating β-Catenin Deubiquitination Researchers found that the β-catenin inhibitory domain (CID) in adenomatous polyposis coli (APC) represents the threshold for pathological levels of Wnt activation and tumor transformation. Mechanistically, CID-deleted APC truncation promotes β-catenin deubiquitination through reverse binding of β-TrCP and USP7 to the destruction complex. [Cell Rep] Abstract , Graphical Abstract , Press Release Identification of a Specific Peptide Binding to Colon Cancer Cells from a Phage-Displayed Peptide Library A peptide termed as CBP-DWS, which was demonstrated to be capable of binding to a panel of human colon cancer cell lines and tissues, was identified; it had ...
Our scientists perform extensive and careful designing of the desired sequence for codon optimization, randomization, and mutation, insertion of reporter gene sequences or tags to facilitate subsequent detection /purification of the desired ligand, cDNA or the antibody. For cDNA phage display libraries, Rx Biosciences uses a novel protocol, which avoids restriction enzyme mediated cDNA truncation, as commonly used by other vendors for cDNA cloning. Hence our protocol enhances the chance of display of full length proteins at the surface of the phages. Rx Biosciences also constructs normalized, subtracted and full-length cDNA libraries in different phage display vectors. We pioneer in recombinant antibody library construction, screening and overexpression for large scale isolation and purification of monoclonal antibodies.. To receive a custom quote, please contact us. We look forward to hearing from you!. Receive a Quote ...
E-selectin is an inducible cell adhesion molecule which mediates rolling of neutrophils as well as adhesion of carcinoma cells to endothelium. Inhibition of selectin-mediated interaction is a possible means for controlling inflammation induced diseases and metastatic spread. The purpose of these studies is to identify peptide forms mimicking Lewis X (LeX), sialyl-Lewis X (SA-LeX), sialyl-Lea (SA-Lea), and Lewis Y (LeY) carbohydrate structures to disrupt lectin-ligand interactions and evaluate their properties to block adenocarcinoma cell adhesion to endothelial cells and tumor metastasis in vitro and in vivo. We used recombinant peptide library to identify novel ligands for E-selectin. We have identified five dodeca peptides mimicking SA-Lea carbohydrate, which is one of the E-selectin ligands, via means of random peptide library screening using SA-Lea-specific monoclonal antibody (MAb) NS 19-9. Peptides with the highest binding affinity for the MAb will be synthesized and characterized for its anti
The cell-extrinsic apoptotic pathway triggers programmed cell death in response to certain ligands that bind to cell-surface death receptors. Apoptosis is essential for normal development and homeostasis in metazoans, and furthermore, selective activation of the cell-extrinsic pathway in tumor cells holds considerable promise for cancer therapy. We used phage display to identify peptides and synthetic antibodies that specifically bind to the human proapoptotic death receptor DR5. Despite great differences in overall size and structure, the DR5-binding peptides and antibodies shared a tripeptide motif, which was conserved within a disulfide-constrained loop of the peptides and the third complementarity determining region of the antibody heavy chains. The X-ray crystal structure of an antibody in complex with DR5 revealed that the tripeptide motif is buried at the core of the interface, confirming its central role in antigen recognition. We found that certain peptides and antibodies exhibited ...