Thiol-Rich fp-6 Controls the Tautomer Equilibrium of Oxidized Dopa in Interfacial Mussel Foot Proteins
SCIE
SCOPUS
- Title
- Thiol-Rich fp-6 Controls the Tautomer Equilibrium of Oxidized Dopa in Interfacial Mussel Foot Proteins
- Authors
- Shin, Mincheol; Yoon, Taehee; Yang, Byeongseon; Cha, Hyung Joon
- Date Issued
- 2022-03
- Publisher
- American Chemical Society
- Abstract
- © 2022 American Chemical Society. All rights reserved.3,4-Dihydroxyphenylalanine (Dopa) is a versatile molecule that enables marine mussels to achieve successful underwater adhesion. However, due to its complicated redox chemistry and vulnerability to oxidation, controlling surface adhesion and cohesion has been a challenging issue to overcome. Foot protein type 6 (fp-6), a thiol-rich interfacial mussel adhesive protein, has been reported as a proteinaceous antioxidant for mussels that helps Dopa maintain surface adhesion ability. In this study, we focused on the role of fp-6 in oxidized Dopa. The effect on the tautomer equilibrium of oxidized Dopa was investigated using recombinant fp-6 (rfp-6) and Dopa-incorporated foot protein type 3 fast variant (drfp-3F), which were produced in bacterial cells. The redox chemistry of Dopa in drfp-3F and the role of rfp-6 were observed using a UV-vis spectrophotometer and a surface forces apparatus (SFA). We discovered that rfp-6 shifts the tautomer equilibrium to ΔDopa as a preferred tautomer for oxidized Dopa in drfp-3F and makes drfp-3F better on underwater surface adhesion.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/112949
- DOI
- 10.1021/acs.langmuir.1c03239
- ISSN
- 0743-7463
- Article Type
- Article
- Citation
- Langmuir, vol. 38, no. 11, page. 3446 - 3452, 2022-03
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