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Protein- and metal-dependent interactions of a prominent protein in mussel adhesive plaques SCIE SCOPUS

Title
Protein- and metal-dependent interactions of a prominent protein in mussel adhesive plaques
Authors
Hwang, DSHongbo ZengAdmir MasicMatthew J. HarringtonJacob N. IsraelachviliJ. Herbert Waite
Date Issued
2010-08-13
Publisher
The American Society for Biochemistry and Molecular Biology
Abstract
The adhesive plaques of Mytilus byssus are investigated increasingly to determine the molecular requirements for wet adhesion. Mfp-2 is the most abundant protein in the plaques, but little is known about its function. Analysis of Mfp-2 films using the surface forces apparatus detected no interaction between films or between a film and bare mica; however, addition of Ca2+ and Fe3+ induced significant reversible bridging (work of adhesion W-ad approximate to 0.3 mJ/m(2) to 2.2 mJ/m(2)) between two films at 0.35 M salinity. The strongest observed Fe3+-mediated bridging approaches the adhesion of oriented avidin-biotin complexes. Raman microscopy of plaque sections supports the co-localization of Mfp-2 and iron, which interact by forming bis- or tris-DOPA-iron complexes. Mfp-2 adhered strongly to Mfp-5, a DOPA-rich interfacial adhesive protein, but not to another interfacial protein, Mfp-3, which may in fact displace Mfp-2 from mica. In the presence of metal ions or Mfp-5, Mfp-2 adhesion was fully reversible. These results suggest that plaque cohesiveness depends on Mfp-2 complexation of metal ions, particularly Fe3+ and also by Mfp-2 interaction with Mfp-5 at the plaque-substratum interface.
Keywords
EPIDERMAL-GROWTH-FACTOR; NUCLEAR-MAGNETIC-RESONANCE; MYTILUS-EDULIS; CROSS-LINKING; BYSSAL THREADS; FOOT PROTEINS; BLUE MUSSEL; SURFACES; DOPA; CALIFORNIANUS
URI
https://oasis.postech.ac.kr/handle/2014.oak/25713
DOI
10.1074/JBC.M110.133157
ISSN
0021-9258
Article Type
Article
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 285, no. 33, page. 25850 - 25858, 2010-08-13
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황동수HWANG, DONG SOO
Div of Environmental Science & Enginrg
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