Recent developments in retro peptides and proteins--an ongoing topochemical exploration. NLM AIDSLINE Important note: Information in this article was accurate in 1996. The state of the art may have changed since the publication date.

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Recent developments in retro peptides and proteins--an ongoing topochemical exploration.

Trends Biotechnol. 1995 Oct;13(10):438-45. Unique Identifier : AIDSLINE MED/96030282
Chorev M; Goodman M; Department of Pharmaceutical Chemistry, Faculty of Medicine,; Hebrew University, Jerusalem, Israel.

Abstract: Main-chain peptidomimetics based on peptide-bond reversal and inversion of chirality represent important structural alterations for peptides and proteins, and are highly significant for biotechnology; these modifications have been widely applied: the D-HIV-protease dimer cleaves only all-D substrate; an all-D-hexapeptide opioid is able to produce analgesia following intraperitoneal administration. Antigenicity and immunogenicity can be achieved by metabolically stable antigens such as all-D- and retro-inverso-isomers of natural antigenic peptides. Isomers, including the retro- and retro-inverso- forms, of hybrid peptides derived from cercropin A and melittin, maintain antimicrobial activity. Therefore, an insight is provided into structure-activity relationships and the rational design of biologically important isomeric peptides.
Keywords: Amino Acid Sequence HIV Protease/CHEMISTRY Molecular Sequence Data Narcotics/CHEMISTRY *Protein Conformation Stereoisomers Structure-Activity Relationship Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. JOURNAL ARTICLE REVIEW REVIEW, TUTORIAL

KWDaminoacidsequencehivprotease/chemistrymolecularsequencedatanarcotics/chemistryKWDproteinconformationstereoisomersstructure-activityrelationshipsupport,non-uKWDsKWDgov'tsupport,uKWDsKWDgov't,pKWDhKWDsKWDjournalarticlereviewreview,tutorial
960130
M9610765

Copyright © 1996 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

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