Molecular interactions of mussel protective coating protein, mcfp-1, from Mytilus californianus
SCIE
SCOPUS
- Title
- Molecular interactions of mussel protective coating protein, mcfp-1, from Mytilus californianus
- Authors
- Qingye Lu; Hwang, DS; Yang Liu; Hongbo Zeng
- Date Issued
- 2012-02
- Publisher
- Elsevier B.V.
- Abstract
- Protective coating of the byssus of mussels (Mytilus sp.) has been suggested as a new paradigm of medical coating due to its high extensibility and hardness co-existence without their mutual detriment. The only known biomacromolecule in the extensible and tough coating on the byssus is mussel foot protein-1 (mfp-1), which is made up with positively charged residues (similar to 20 mol%) and lack of negatively charged residues. Here, adhesion and molecular interaction mechanisms of Mytilus californianus foot protein-1 (mcfp-1) from California blue mussel were investigated using a surface forces apparatus (SFA) in buffer solutions of different ionic concentrations (0.2-0.7 M) and pHs (3.0-5.5). Strong and reversible cohesion between opposed positively charged mcfp-1 films was measured in 0.1 M sodium acetate buffer with 0.1 M KNO3. Cohesion of mcfp-1 was gradually reduced with increasing the ionic strength, but was not changed with pH variations. Oxidation of 3,4-dihydroxyphenylalanine (DOPA) residues of mcfp-1, a key residue for adhesive and coating proteins of mussel, didn't change the cohesion strength of mcfp-1 films, but the addition of chemicals with aromatic groups (i.e., aspirin and 4-methylcatechol) increased the cohesion. These results suggest that the cohesion of mcfp-1 films is mainly mediated by cation-it interactions between the positively charged residues and benzene rings of DOPA and other aromatic amino acids (similar to 20 mol% of total amino acids of mcfp-1), and pi-pi interactions between the phenyl groups in mcfp-1. The adhesion mechanism obtained for the mcfp-1 proteins provides important insight into the design and development of functional biomaterials and coatings mimicking the extensible and robust mussel cuticle coating. (C) 2011 Elsevier Ltd. All rights reserved.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/17035
- DOI
- 10.1016/J.BIOMATERIALS.2011.11.021
- ISSN
- 0142-9612
- Article Type
- Article
- Citation
- BIOMATERIALS, vol. 33, no. 6, page. 1903 - 1911, 2012-02
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