Adsorption of the fusogenic peptide B18 onto solid surfaces: insights into the mechanism of peptide assembly.
The adsorption and assembly of B18 peptide on various solid surfaces were studied by reflectometry techniques and atomic force microscopy. B18 is the minimal membrane binding and fusogenic motif of the sea urchin protein bindin, which mediates the fertilization process. Silicon substrates were modified to obtain hydrophilic charged surfaces (oxide layer and polyelectrolyte multilayers) and hydrophobic surfaces (octadecyltrichlorosilane). B18 does not adsorb on hydrophilic positively charged surfaces, which was attributed to electrostatic repulsion since the peptide is positively charged. In contrast, the peptide irreversibly adsorbs on negatively charged hydrophilic as well as on hydrophobic surfaces. B18 showed higher affinity for hydrophobic surfaces than for hydrophilic negatively charged surfaces, which must be due to the presence of hydrophobic side chains at both ends of the molecule. Atomic force microscopy provided the indication that lateral diffusion on the surface affects the adsorption process of B18 on hydrophobic surfaces. The adsorption of the peptide on negatively charged surfaces was characterized by the formation of globular clusters.
Rocha
Sandra
S
Max Planck Institute of Colloids and Interfaces, Research Campus Golm, Am Mühlenberg 1, D-14476 Potsdam, Germany.
Pereira
M Carmo
MC
Coelho
Manuel A N
MA
Möhwald
Helmuth
H
Brezesinski
Gerald
G
D000327:Adsorption; D057927:Hydrophobic and Hydrophilic Interactions; D018625:Microscopy, Atomic Force / Q000379:methods*; D010316:Particle Size; D010455:Peptides / Q000737:chemistry*; D012680:Sensitivity and Specificity; D013499:Surface Properties; D013997:Time Factors
D010455:Peptides