한빛사논문, 상위피인용논문
- 조회6,141
Abstract
, and Phillip B. Messersmith *
Departments of *Biomedical Engineering and Materials Science and Engineering, Northwestern University, 2145 Sheridan Road, Evanston, IL 60208; and Department of Chemistry and Institute for Biophysical Dynamics, University of Chicago, 5735 South Ellis Avenue, Chicago, IL 60637
Communicated by George C. Schatz, Northwestern University, Evanston, IL, July 3, 2006 (received for review April 5, 2006)
The glue proteins secreted by marine mussels bind strongly to virtually all inorganic and organic surfaces in aqueous environments in which most adhesives function poorly. Studies of these functionally unique proteins have revealed the presence of the unusual amino acid 3,4-dihydroxy-L-phenylalanine (dopa), which is formed by posttranslational modification of tyrosine. However, the detailed binding mechanisms of dopa remain unknown, and the chemical basis for mussels'' ability to adhere to both inorganic and organic surfaces has never been fully explained. Herein, we report a single-molecule study of the substrate and oxidation-dependent adhesive properties of dopa. Atomic force microscopy (AFM) measurements of a single dopa residue contacting a wet metal oxide surface reveal a surprisingly high strength yet fully reversible, noncovalent interaction. The magnitude of the bond dissociation energy as well as the inability to observe this interaction with tyrosine suggests that dopa is critical to adhesion and that the binding mechanism is not hydrogen bond formation. Oxidation of dopa, as occurs during curing of the secreted mussel glue, dramatically reduces the strength of the interaction to metal oxide but results in high strength irreversible covalent bond formation to an organic surface. A new picture of the interfacial adhesive role of dopa emerges from these studies, in which dopa exploits a remarkable combination of high strength and chemical multifunctionality to accomplish adhesion to substrates of widely varying composition from organic to metallic.
Author contributions: P.B.M. designed research; H.L. performed research; H.L., N.F.S., and P.B.M. analyzed data; and H.L., N.F.S., and P.B.M. wrote the paper.
Conflict of interest statement: No conflicts declared.
To whom correspondence should be addressed.
논문정보
- Research article
- 2006년 08월 (BRIC 등록일 )
- 국외 연구진
- 바이오·의료융합 > 바이오센싱 및 나노바이오물질
- 60회 이상 인용된 논문 (상위피인용논문 등록일 2009-09-08)
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