Peptide library (original) (raw)
A peptide library is a tool for studying proteins. A peptide library contains a great number of peptides that have a systematic combination of amino acids. Usually, the peptide library is synthesized on a solid phase, mostly on resin, which can be made as a 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. Example: Say you wanted a peptide chain of 10 residues in length to use in native chemical ligation with a larger recombinantly expressed protein.
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| dbo:abstract | A peptide library is a tool for studying proteins. A peptide library contains a great number of peptides that have a systematic combination of amino acids. Usually, the peptide library is synthesized on a solid phase, mostly on resin, which can be made as a 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. Synthetic peptide libraries are synthesized without utilizing phage or other biological systems. At least five subtypes of these libraries exist, and the distinguishing characteristic is the method of synthesis of each library. The subtypes are (1) overlapping peptide libraries, (2) truncation peptide libraries, (3) random libraries, (4) alanine scanning libraries, and (5) positional or scrambled peptide libraries. A mixture of desired amino acids can be created at each point in a sequence. In this way, a library of 20 different polypeptides can be created with only one randomized amino acid residue position with all other positions held constant. The usefulness of this form of peptide synthesis is limited as it is limited to approximately 70 amino acids in length. This would give you 2070 possible combinations and that is only if you do not 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 would not learn very much. Example: Say you wanted a peptide chain of 10 residues in length to use in native chemical ligation with a larger recombinantly expressed protein. Chosen randomly, you want a set of proteins with the following: * Residue 1: alanine * Residue 2: glutamine, glycine, arginine, glutamic acid, serine, or methionine * Residue 3: any one of all 20 amino acids * Residue 4: acetyllysine * Residue 5: alanine * Residue 6: isoleucine * Residue 7: aspartic acid * Residue 8: phenylalanine * Residue 9: acetyllysine * Residue 10: arginine with the carboxy terminal thioester There would be 20 different proteins at residue 3. Each one of those would have 7 different proteins at residue 2. The end result would be or 140 different polypeptides. This peptide library would be useful for analyzing the effect of the post-translational modification acetylation on lysine which neutralizes the positive charge. Having the library of different peptides at residue 2 and 3 would let you see if some change in chemical properties in the N-terminal tail of the ligated protein makes the protein more useful or useful in a different way. As a general formula, if you made a completely random peptide library with n amino acids for each link in the chain with a length of , the total number of possible sequences is . Large random peptide libraries are often used for the synthesis of certain peptide molecules, such as ultra-large chemical libraries for the discovery of high-affinity peptide binders, and an increase in the library size severely affects parameters, such as the synthesis scale, the number of library members, the sequence deconvolution and peptide structure elucidation. So, to address these technical challenges, an algorithm-supported approach to peptide library design based on molecular mass and amino acid diversity is proposed in order to simplify the laborious permutation identification in complex mixtures, when mass spectrometry is used, by avoiding mass redundancy. Some companies, such as Pepscan, and GenScript, manufacture customized peptide libraries. (en) |
| dbo:wikiPageExternalLink | https://web.archive.org/web/20120220085304/http:/www.pbcpeptide.com/Peptide%20Library.htm |
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| dbo:wikiPageWikiLink | dbr:Peptide dbr:Thioester dbr:Glutamic_acid dbr:Glutamine dbr:Glycine dbr:Post-translational_modification dbc:Proteins dbr:Drug_design dbr:Acetyllysine dbr:Alanine dbr:Amino_acids dbr:Protein dbr:Resin dbr:Isoleucine dbr:Arginine dbr:Aspartic_acid dbc:Biochemistry_methods dbr:Phenylalanine dbr:Methionine dbr:Serine dbr:Protein–protein_interactions |
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| dct:subject | dbc:Proteins dbc:Biochemistry_methods |
| gold:hypernym | dbr:Tool |
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| rdfs:comment | A peptide library is a tool for studying proteins. A peptide library contains a great number of peptides that have a systematic combination of amino acids. Usually, the peptide library is synthesized on a solid phase, mostly on resin, which can be made as a 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. Example: Say you wanted a peptide chain of 10 residues in length to use in native chemical ligation with a larger recombinantly expressed protein. (en) |
| rdfs:label | Peptide library (en) |
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