Glycosylated Hydroxytryptophan in a Mussel Adhesive Protein from Perna viridis
SCIE
SCOPUS
- Title
- Glycosylated Hydroxytryptophan in a Mussel Adhesive Protein from Perna viridis
- Authors
- Zhao, H; Sagert, J; Hwang, DS; J Herbert Waite
- Date Issued
- 2009-08-28
- Publisher
- American Society for Biochemistry and Molecular Biology
- Abstract
- 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.
- Keywords
- AMINO-ACID-ANALYSIS; C-MANNOSYLATION; PROTECTIVE-COATINGS; CROSS-LINKING; GREEN MUSSEL; TRYPTOPHAN; 5-HYDROXYTRYPTOPHAN; LINKAGE; MIMICS
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/25704
- DOI
- 10.1074/JBC.M109.022517
- ISSN
- 0021-9258
- Article Type
- Article
- Citation
- JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 283, no. 35, page. 23344 - 23352, 2009-08-28
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.