Enhanced biopotency of synthetic C3a analogues by membrane binding. A fluorescence anisotropy decay study.
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.
Federwisch
M
M
Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Germany.
Casaretto
M
M
Gerardy-Schahn
R
R
Bitter-Suermann
D
D
Wollmer
A
A
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
D009842:Oligopeptides; D015926:Complement C3a