The Adhesion Mechanism of Marine Mussel Foot Protein: Adsorption of L-Dopa on α- and β-Cristobalite Silica Using Density Functional Theory

Journal of Chemistry. 2017;2017 DOI 10.1155/2017/8756519

 

Journal Homepage

Journal Title: Journal of Chemistry

ISSN: 2090-9063 (Print); 2090-9071 (Online)

Publisher: Hindawi Limited

LCC Subject Category: Science: Chemistry

Country of publisher: United Kingdom

Language of fulltext: English

Full-text formats available: PDF, HTML, ePUB

 

AUTHORS

Shabeer Ahmad Mian (Department of Physics, University of Peshawar, Peshawar, Pakistan)
Younas Khan (Department of Physics, University of Peshawar, Peshawar, Pakistan)

EDITORIAL INFORMATION

Blind peer review

Editorial Board

Instructions for authors

Time From Submission to Publication: 16 weeks

 

Abstract | Full Text

Marine mussels strongly adhere to various surfaces and endure their attachment under a variety of conditions. In order to understand the basic mechanism involved, we study the adsorption of L-dopa molecule on hydrophilic geminal and terminal isolated silanols of silica (001) surface. High content of modified amino acid L-dopa is found in the glue-like material secreted by the mussels through which it sticks to various surfaces under water. To understand the adsorption behavior, we have made use of periodic Density Functional Theory (DFT) study. The L-dopa molecule adheres to silica surfaces terminated with geminal and terminal silanols via its catechol part. In both cases, the adhesion is achieved through the formation of 4 H-bonds. A binding energy of 29.48 and 31.67 kcal/mol has been estimated, after the inclusion of dispersion energy, for geminal and terminal silanols of silica, respectively. These results suggest a relatively stronger adhesion of dopa molecule for surface with terminal isolated silanols.