title: Role of the backbone conformation at position 7 in the structure and activity of marinostatin, an ester-linked serine protease inhibitor.
abstract: Rational design of inhibitors: The cis-amide backbone at position 7 in the serine protease inhibitor marinostatin was replaced with an E or Z olefin. The E olefin analogue was not active, but the Z analogue was. The cis conformation might play a critical role in organizing a canonical structure for binding to proteases.
authors.affiliation: SAITO Research Center, Peptide Institute, Inc. 7-2-9 Saito-Asagi, Ibaraki, Osaka, Japan.
authors.forename: Misako
authors.initials: M
authors.lastname: Taichi
authors.forename: Toshimasa
authors.initials: T
authors.lastname: Yamazaki
authors.forename: Yuji
authors.initials: Y
authors.lastname: Nishiuchi
mesh_terms: D000475:Alkenes / Q000737:chemistry / Q000494:pharmacology; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008968:Molecular Conformation; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000494:pharmacology*; D031161:Pseudoalteromonas / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D013381:Subtilisins / Q000037:antagonists & inhibitors* / Q000378:metabolism
chemical_list: D000475:Alkenes; D010456:Peptides, Cyclic; D015842:Serine Proteinase Inhibitors; C577199:marinostatin; D013381:Subtilisins