Siderophores and mussel foot proteins: the role of catechol, cations, and metal coordination in surface adhesion.

TitleSiderophores and mussel foot proteins: the role of catechol, cations, and metal coordination in surface adhesion.
Publication TypeJournal Article
Year of Publication2017
AuthorsMaier GP, Butler A
JournalJ Biol Inorg Chem
Date Published2017 Jul

Metal coordination, hydrogen bonding, redox reactions, and covalent crosslinking are seemingly disparate chemical and physicochemical processes that are all accomplished in natural materials by the catechol functional group. This review focuses on the reactivity of catechols in tris-2,3-dihydroxybenzoyl-containing microbial siderophores and synthetic analogs, as well as Dopa-(3,4-dihydroxyphenylalanine)-containing mussel foot proteins that adhere to surfaces in aqueous conditions. Mussel foot proteins with a high content of Dopa and cationic amino acids, Lys and Arg, adhere strongly to mica, an aluminosilicate mineral, in aqueous conditions. The siderophore cyclic trichrysobactin, tris-(2,3-dihydroxybenzoyl-D-Lys-L-Ser) and related synthetic analogs in which the tri-Ser macrolactone is replaced by Tren, tris-(2-aminoethyl)amine, also adheres strongly to mica. Variation in the nature of the catechol and cationic groups in synthetic analogs reveals a synergism between the cationic amino acid and the catechol, required for strong aqueous adhesion. Autoxidation and iron(III)-catalyzed oxidation of 2,3-dihydroxy and 3,4-dihydroxy catechols are also considered. These siderophore analogs provide a platform to understand catechol interactions and reactivity on surfaces, which may ultimately improve the design of synthetic materials that address diverse challenges in medicine, materials science, as well as other disciplines, in which surface adhesion in aqueous conditions is important.

Alternate JournalJ. Biol. Inorg. Chem.
PubMed ID28364222