Annexin V membrane interaction: an electrostatic potential study

✍ Scribed by Andrej Karshikov; Robert Berendes; Alexander Burger; Adolfo Cavalié; Hans-Dieter Lux; Robert Huber

• Book ID: 104659225
• Publisher: Springer
• Year: 1992
• Tongue: English
• Weight: 720 KB
• Volume: 20
• Category: Article
• ISSN: 1432-1017
• DOI: 10.1007/bf00196592

✦ Synopsis

The possible role of electrostatic interactions for membrane binding and pore formation of annexin V has been analysed on the basis of a simple dielectric model. It is suggested that the binding of phospholipids to annexin V is regulated, at least initially, by the protein's electrostatic potential. The calculations show that a strong local gradient of the electrostatic potential exists at the membrane-protein interface and a membrane pore may be generated by electroporation. The observed specificity and regulation of ion conduction is suggested to reside in the protein part of the pore. On the basis of the three-dimensional structures of the protein and its hypothetical membrane complex, and electrophysiological measurements, a mechanical model of the transmembrane voltage regulation of the annexin's ion conduction properties is proposed.