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Peptide libraries are vital tools in drug development because most drugs rely on protein-protein interactions to disrupt or trigger specific processes. Truncation libraries are one important strategy used by researchers to pinpoint essential residues on the interface landscape.
These libraries are designed by systematically trimming (truncation) flanking amino acid residues from each terminus of an active protein segment. By screening the activity of increasingly shorter peptides, researchers can unveil the role of adjacent residues and determine the minimum length of a peptide required for activity.
To get more out of your truncation library experiments, it is fundamental to identify key segments within the protein through alanine scanning studies prior to truncation. To streamline design and testing, ProteoGenix developed an intuitive tool for the instant generation of truncation peptide libraries and corresponding quotes.
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Truncation peptide libraries are commonly used to determine the minimal binding site of a protein. The information derived from these experiments allows for multiple applications, namely:
In vaccine development, truncation peptide libraries have been recurrently used to elicit the generation of protective antibodies against epitopes common to several serological variants of a specific pathogen. The most noteworthy example is Group A Streptococcus (GAS), in which the minimal B cell epitope, conserved among several variants, was found to be only 12 amino acids long.
Truncation libraries can also help find minimum epitopes with substantially different properties compared to those of the parental peptide. Truncated peptides often interact distinctly with the target protein precisely because they can fit into binding pockets that had not been previously characterized. This strategy can serve as a starting point for drug discovery by modifying the mode of action of the parental peptide and allowing the inhibition of new druggable targets.
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