期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 284, 期 35, 页码 23344-23352出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109.022517
关键词
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资金
- National Institutes of Health [R01 DE018468]
- National Science Foundation [MRSEC DMR05-20415]
The 3,4-dihydroxyphenyl-L-alanine (Dopa)-containing proteins of mussel byssus play a critical role in wet adhesion and have inspired versatile new synthetic strategies for adhesives and coatings. Apparently, however, not all mussel adhesive proteins are beholden to Dopa chemistry. The cDNA-deduced sequence of Pvfp-1, a highly aromatic and redox active byssal coating protein in the green mussel Perna viridis, suggests that Dopa may be replaced by a post-translational modification of tryptophan. The N-terminal tryptophan-rich domain of Pvfp-1 contains 42 decapeptide repeats with the consensus sequences ATPKPW(1)TAW(2)K and APPPAW(1)TAW(2)K. A small collagen domain (18 Gly-X-Y repeats) is also present. Tandem mass spectrometry of isolated tryptic decapeptides has detected both C-2-hexosylated tryptophan(W-1) and C-2-hexosylated hydroxytryptophan (W-2), the latter of which is redox active. The UV absorbance spectrum of W-2 is consistent with 7-hydroxytryptophan, which represents an intriguing new theme for bioinspired opportunistic wet adhesion.
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