Journal
BIOMACROMOLECULES
Volume 17, Issue 3, Pages 946-953Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biomac.5b01622
Keywords
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Funding
- National Research Foundation of Korea Grant - Ministry of Science, ICT and Future Planning (MSIP) [NRF2014R1A2A2A01006724, NRF-C1ABA001-2011-0029960]
- NSERC Discovery Grant
- NSERC RTI Grant from the Natural Sciences and Engineering Research Council of Canada
- Marine Biotechnology Program (Marine BioMaterials Research Center) - Ministry of Oceans and Fisheries, Korea [D11013214H480000110]
- Global Ph.D. Fellowship Program through the National Research Foundation of Korea [NRF-2011-0008261]
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Recent works on mussel adhesion have identified a load bearing matrix protein (PTMP1) containing von Willebrand factor (vWF) with collagen binding capability that contributes to the mussel holdfast by manipulating mussel collagens. Using a surface forces apparatus, we investigate for the first time, the nanomechanical properties of vWF-collagen interaction using homologous proteins of mussel byssus, PTMP1 and preCollagens (preCols), as collagen. Mimicking conditions similar to mussel byssus secretion (pH < 5.0) and seawater condition (pH 8.0), PTMP1 and preCol interact weakly in the positioning phase based on vWF-collagen binding and strengthen in locked phase due to the combined effects of electrostatic attraction, metal binding, and mechanical shearing. The progressive enhancement of binding between PTMP1 with porcine collagen under the aforementioned conditions is also observed. The binding mechanisms of PTMP1-preCols provide insights into the molecular interaction of the mammalian collagen system and the development of an artificial extracellular matrix based on collagens.
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