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Adhesion of Mytilus Edulis Foot Protein 1 on Silica: Ionic Effects on Biofouling

Brian P Frank, Georges Belfort

Biotechnol Prog. May-Jun 2002;18(3):580-6.

PMID: 12052076

Abstract:

To determine the effect of the ionic environment on the marine adhesion molecule Mytilus edulis foot protein 1 (Mefp-1), atomic force microscopy (AFM) was used to measure the adhesion between Mefp-1 and a silica substrate under a range of ionic conditions. Both ion strength and type were varied on the basis of the ions present in natural seawater. Salts containing monovalent ions (NaCl, KCl) increased adhesion only slightly, but salts containing divalent ions (MgCl(2), CaCl(2), Na(2)SO(4)) induced multiple jumpouts in the decompression curve similar to other biological systems and an increase in hydrodynamic radius as observed by light scattering. This behavior may be due to metal complexation between 3,4-dihydroxyphenyl-L-alanine and o-quinone catechol groups on Mefp-1. The addition of a salt containing a trivalent ion (FeCl(3)) resulted in the highest adhesion. The strong effect of salt type and concentration suggests that the ionic composition of the environment within the mussel byssus may be tailored in order to achieve maximum adhesion and minimum curing time.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
LS74801 Mytilus edulis foot protein-1 Mytilus edulis foot protein-1 Price
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