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Peptide self-aggregation and peptide complementarity as bases for the evolution of peptide receptors: a review

✍ Scribed by Robert S. Root-Bernstein

Publisher: John Wiley and Sons
Year: 2005
Tongue: English
Weight: 142 KB
Volume: 18
Category: Article
ISSN: 0952-3499
DOI: 10.1002/jmr.690

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✦ Synopsis

This paper reviews the three major theories of peptide receptor evolution: (1) Dwyer's theory that peptide receptors evolved from self-aggregating peptides; (2) Root-Bernstein's theory that peptide receptors evolved from functionally and structurally complementary peptides; and (3) Blalock's theory that receptors evolved from hydropathically complementary sequences encoded in the antisense strand of the DNA encoding each peptide. The evidence to date suggests that the co-evolution of peptides and their receptors is strongly constrained by one or more of these physicochemically based mechanisms, which argues against a random or 'frozen accident' model. The data also suggest that structure and function are integrally related from the earliest steps of receptor-ligand evolution so that peptide functionality is non-random and highly conserved in its origin. The result is a 'molecular paleontology' that reveals the evolutionary constraints that shaped the interaction of structure and function.

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