期刊
ACS APPLIED MATERIALS & INTERFACES
卷 9, 期 13, 页码 11493-11505出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsami.7b01185
关键词
barnacles; bioadhesion; biofouling; catechol oxidation; lysyl oxidase; peroxidase; protein cross-linking; chemical modification
资金
- Office of Naval Research through the Naval Research Laboratory Base Program
- Office of Naval Research through ONR Coatings Program at NRL [N0001415WX01915]
- Office of Naval Research through ONR Coatings Program at Duke [N000141110180/N000141210365]
- National Research Council Post Doctoral Associate
- Naval Research Enterprise Internship Program
- Summer Engineering Apprentice Program at NRL
Oxidases are found to play a growing role in providing functional chemistry to marine adhesives for the permanent attachment of macrofouling organisms. Here, we demonstrate active peroxidase and lysyl oxidase enzymes in the adhesive layer of adult Amphibalanus amphitrite barnacles through live staining, proteomic analysis, and competitive enzyme assays on isolated cement. A novel full-length peroxinectin (AaPxt-1) secreted by barnacles is largely responsible for oxidizing phenolic chemistries; AaPxt-1 is driven by native hydrogen peroxide in the adhesive and oxidizes phenolic substrates typically preferred by phenoloxidases (POX) such as laccase and tyrosinase. A major cement protein component AaCP43 is found to contain ketone/aldehyde modifications via 2,4-dinitrophenylhydrazine (DNPH) derivatization, also called Bradys reagent, of cement proteins and immunoblotting with an anti-DNPH antibody. Our work outlines the landscape of molt-related oxidative pathways exposed to barnacle cement proteins, where ketone- and aldehyde-forming oxidases use peroxide intermediates to modify major cement components such as AaCP43.
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