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Sequence shuffle controls morphological consequences in a self‐assembling tetrapeptide
Author(s) -
Joshi K. B.,
Verma Sandeep
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.955
Subject(s) - tetrapeptide , supramolecular chemistry , peptide , amino acid , sequence (biology) , chemistry , hydrogen bond , context (archaeology) , linker , peptide sequence , stereochemistry , crystallography , biochemistry , molecule , biology , crystal structure , organic chemistry , computer science , paleontology , gene , operating system
Abstract Peptide and protein self‐assembly is a well‐studied phenomenon in chemistry and biology, where nanoscopic building blocks exhibit rapid self‐association to reveal supramolecular aggregates of defined structural features. These superstructures are stabilized by hydrophobic interactions, hydrogen bonding and a host of other noncovalent interactions. Thus, amino acid side chains in the primary structure hold importance in dictating secondary structures and preference for particular conformational signatures in peptide aggregates. This report describes contrasting nanoscale morphologies in antamanide‐derived synthetic tetrapeptide mutants, which are composed by shuffling only two amino acids: phenylalanine and proline. Remarkable differences in ultrastructures in primary sequence‐shuffled tetrapeptides suggest dissimilar aggregational pathways due to context‐dependent location of proline and phenylalanine residues with respect to one another. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.