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).