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Isosteric replacement of sulfur with other chalcogens in peptides and proteins
Author(s) -
Moroder Luis
Publication year - 2005
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.654
Subject(s) - selenocysteine , diselenide , chemistry , chalcogen , amino acid , cysteine , cystine , selenium , serine , methionine , biochemistry , peptide , combinatorial chemistry , enzyme , organic chemistry
Abstract The review addresses the functional and structural properties of the two series of chalcogen analogues of amino acids in peptides and proteins, the methionine and the serine/cysteine series, and discusses the synthesis of the related selenium/tellurium analogues as well as their use in peptide synthesis and protein expression. Advances in synthetic methodologies and recombinant technologies and their combined applications in native and expressed protein ligation allows the isomorphous character of selenium‐ and tellurium‐containing amino acids to be exploited for production of heavy metal mutants of proteins and thus to facilitate the phasing problem in x‐ray crystallography. In addition, selenocysteine has been recognized as an ideal tool for the production of selenoenzymes with new catalytic activities. Moreover, the fully isomorphous character of disulfide replacement with diselenide is well suited to increase the robustness of cystine frameworks in cystine‐rich peptides and proteins and for the de novo design of even non‐native cystine frameworks by exploiting the highly negative redox potential of selenols. Copyright © 2005 European Peptide Society and John Wiley & Sons, Ltd.