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Titolo:
DESIGN OF PEPTIDES, PROTEINS, AND PEPTIDOMIMETICS IN CHI-SPACE
Autore:
HRUBY VJ; LI GG; HASKELLLUEVANO C; SHENDEROVICH M;
Indirizzi:
UNIV ARIZONA,DEPT CHEM TUCSON AZ 85721
Titolo Testata:
Biopolymers
fascicolo: 3, volume: 43, anno: 1997,
pagine: 219 - 266
SICI:
0006-3525(1997)43:3<219:DOPPAP>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
UNUSUAL AMINO-ACIDS; OPTICALLY PURE ISOMERS; SIDE-CHAIN CONFORMATION; ASYMMETRIC-SYNTHESIS; STEREOSELECTIVE SYNTHESIS; BETA-METHYLPHENYLALANINE; SOMATOSTATIN ANALOGS; BIOLOGICAL-ACTIVITY; ALPHA-MELANOTROPIN; METHYL-1,2,3,4-TETRAHYDROISOQUINOLINE-3-CARBOXYLIC ACID;
Keywords:
PEPTIDES; PROTEINS; PEPTIDOMIMETICS; CHI SPACE;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
176
Recensione:
Indirizzi per estratti:
Citazione:
V.J. Hruby et al., "DESIGN OF PEPTIDES, PROTEINS, AND PEPTIDOMIMETICS IN CHI-SPACE", Biopolymers, 43(3), 1997, pp. 219-266

Abstract

Peptide and protein biological activities depend on their three dimensionals structures in the free state and when interacting with their receptors/acceptors. The backbone conformations such as alpha-helix, beta-sheet, beta-turn, and so forth provide critical templates for the three-dimensional structure, but the overall shape and intrinsic stereoelectronic properties of the peptide or protein important for molecular recognition, signal transduction, enzymatic specificity, immunomodulation, and other biological effects depend on arrangement of the side chain groups in three-dimensional chi space (their chi(1), chi(2), etc. torsional angles). In this paper we explore approaches to the de novo design of polypeptides and peptidomimetics with biased or specific conformational/topographical properties in chi space. We consider computational and experimental methods that can be used to examine the effects of specific structural modifications in constraining side chain groups of amino acid residues and their similarities in chi space to thenatural amino acids to evaluate what sort of mimetics are likely to minic normal amino acids. We then examine some of the asymmetric synthetic methods that are being developed to obtain the amino acid mimetics. Finally, we consider selected examples in the literature where thesespecialized amino acids have been incorporated in biologically activepeptides and the specific insights they have provided regarding the topographical requirements for bioactive peptide potency, selectivity, and other biochemical and pharmacological properties. Constraints in chi space show great promise as useful tools in peptide, protein, and peptidomimetic de novo design of structures and pharmacophores with specific stereostructural, biochemical and biological properties. (C) 1997 John Wiley & Sons, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 00:20:00