title: Enhanced biopotency of synthetic C3a analogues by membrane binding. A fluorescence anisotropy decay study.
abstract: The biological activity of oligopeptide analogues of C3a is markedly increased by N-terminal attachment of a hydrophobic group as, for instance, 9-fluorenylmethoxycarbonyl (Fmoc), either direct or via a flexible 6-aminohexanoyl (Ahx) spacer. This study presents evidence from fluorescence anisotropy decay measurements that the hydrophobic appendix mediates non-specific binding of the synthetic peptide analogues to phospholipid vesicles. According to quantitative considerations no alternative or additional rate-enhancing mechanisms other than surface diffusion are required to account for the gain in biopotency.
authors.affiliation: Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Federwisch
authors.forename: M
authors.initials: M
authors.lastname: Casaretto
authors.forename: R
authors.initials: R
authors.lastname: Gerardy-Schahn
authors.forename: D
authors.initials: D
authors.lastname: Bitter-Suermann
authors.forename: A
authors.initials: A
authors.lastname: Wollmer
mesh_terms: D000595:Amino Acid Sequence; D015926:Complement C3a / Q000031:analogs & derivatives* / Q000378:metabolism*; D005454:Fluorescence Polarization / Q000379:methods; D007700:Kinetics; D008433:Mathematics; D008566:Membranes / Q000378:metabolism; D008962:Models, Theoretical; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism; D011485:Protein Binding; D013329:Structure-Activity Relationship
chemical_list: D009842:Oligopeptides; D015926:Complement C3a