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1996-01-30
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Document 0765
DOCN M9610765
TI Recent developments in retro peptides and proteins--an ongoing
topochemical exploration.
DT 9601
AU Chorev M; Goodman M; Department of Pharmaceutical Chemistry, Faculty of
Medicine,; Hebrew University, Jerusalem, Israel.
SO Trends Biotechnol. 1995 Oct;13(10):438-45. Unique Identifier : AIDSLINE
MED/96030282
AB 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.
DE 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
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).