Recent developments in retro peptides and proteins--an ongoing topochemical exploration.
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.
Chorev
M
M
Department of Pharmaceutical Chemistry, Faculty of Medicine, Hebrew University, Jerusalem, Israel.
Goodman
M
M
D000595:Amino Acid Sequence; D016333:HIV Protease / Q000737:chemistry; D008969:Molecular Sequence Data; D009294:Narcotics / Q000737:chemistry; D011487:Protein Conformation; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D009294:Narcotics; D016333:HIV Protease