Resumen

PATIL, Navinkumar J; VINUEZA NARANJO, Paola Gabriela  y  ZAPPONE, Bruno. Wet Adhesive Properties of Asian Green Mussel (Perna viridis) Foot Protein Pvfp-5: An Underwater Adhesive Primer. Novasinergia [online]. 2018, vol.1, n.2, pp.90-99.  Epub 01-Jun-2021. ISSN 2631-2654.  https://doi.org/10.37135/unach.ns.001.02.10.

Asian green mussels (Perna viridis) are bivalves that attach firmly to rocks in wave-battered intertidal seashores via a proteinaceous secretion. P. viridis mussels follow a precisely time-regulated secretion of adhesive proteins where P. viridis foot protein-5 (Pvfp-5) was identified as the first protein to be secreted during the formation of adhesive plaque. The high content of catecholic amino acid 3,4-dihydroxy-L-phenylalanine (DOPA) ((11 mol%) and cysteine (Cys) ((15 mol%) in Pvfp-5 and its localization near the plaque-substrate interface have prompted speculation that the vanguard protein Pvfp-5 plays a key role as an adhesive primer in underwater adhesion of P. viridis mussels. Surface Force Apparatus (SFA) was used to probe the adhesive properties of Pvfp-5 at the nano-scale where pH dependent wet adhesion and antioxidant activity of foot-extracted and purified Pvfp-5 were investigated. The study revealed that Pvfp-5 with its high DOPA and CYS-content maintains adhesion even at higher pH by overcoming the spontaneous oxidation of DOPA to quinone. SFA results are consistent with the apparent function of Pvfp-5 acting as an adhesive primer, overcoming repulsive hydration forces by displacing surface-bound water and generating strong and durable surface adhesion. Our findings reveal molecular-scale insights that should prove relevant and impact material sciences to help the development of new generation of wet-resistant adhesives, coatings and glues for biomedical, therapeutic and antifouling applications.

Palabras clave : Cisteína (CYS); Dihidroxi-L-fenilalanina (DOPA); Proteínas del pie de mejillón (Mfps); Perna viridis proteína del pie (Pvfp); Aparato de fuerzas de superficie (SFA).

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