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.
Keywords: Protein Binding, peptide synthesis
Protein & Peptide Letters
Title: Rational and Random Strategies for the Mimicry of Discontinuous Protein Binding Sites
Volume: 11 Issue: 4
Author(s): Jutta Eichler
Affiliation:
Keywords: Protein Binding, peptide synthesis
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.
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Cite this article as:
Eichler Jutta, Rational and Random Strategies for the Mimicry of Discontinuous Protein Binding Sites, Protein & Peptide Letters 2004; 11 (4) . https://dx.doi.org/10.2174/0929866043406931
DOI https://dx.doi.org/10.2174/0929866043406931 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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