Rational and random strategies for the mimicry of discontinuous protein binding sites.

Abstract:

:The high technical standard of current peptide chemistry, which has evolved over the past three decades, has profoundly facilitated the investigation of proteins and their interactions with other molecules at the level of individual amino acids. Using currently available peptide synthesis methods, sequentially continuous protein binding sites can be readily mapped, characterized, optimized, and used as lead compounds for inhibitors of protein-ligand interactions. The mimicry of sequentially discontinuous protein binding sites, on the other hand, continues to present a challenge for peptide and organic chemists. This mini-review summarizes currently used and emerging, rational and random strategies for the design of synthetic mimetics of discontinuous protein binding sites.

journal_name

Protein Pept Lett

authors

Eichler J

doi

10.2174/0929866043406931

subject

Has Abstract

pub_date

2004-08-01 00:00:00

pages

281-90

issue

4

eissn

0929-8665

issn

1875-5305

journal_volume

11

pub_type

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