Rational and Random Strategies for the Mimicry of Discontinuous Protein Binding Sites

Author(s): Jutta Eichler.

Journal Name: Protein & Peptide Letters

Volume 11 , Issue 4 , 2004

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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

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Article Details

Year: 2004
Page: [281 - 290]
Pages: 10
DOI: 10.2174/0929866043406931
Price: $65

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