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Electrochemical impedance spectroscopy reveals new mechanism based on competitive binding between Tris and protein on conductive biomimetic polydopamine surface.

Abstract

A novel mechanism was developed to study the interaction of mussel inspired polydopamine surfaces with bovine serum albumin using cyclic voltammetry and electrochemical Impedance spectroscopy supplemented with XPS, IR, UV and Atomic Force microscopy. The polydopamine surfaces reveal different mechanism that gives a new insight in understanding the interaction with BSA under variable conditions used for PDA preparation and BSA adsorption. The study provides in-depth analysis of orientations and interactions of BSA with polydopamine surfaces. The protein interaction behavior changed significantly with different environment including pH and concentration of buffer and thus reveals a competitive binding mechanism of protein binding. The study provides an outlook for studying the interaction of protein foulants with PDA which should be carried out in nucleophilic buffers while the covalent binding or immobilization of the biomolecules to PDA surfaces should be carried out in non-nucleophilic buffer for higher efficiency.

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Publication details

The article was accepted on 14 Sep 2018 and first published on 14 Sep 2018


Article type: Paper
DOI: 10.1039/C8CP05391J
Citation: Phys. Chem. Chem. Phys., 2018, Accepted Manuscript
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    Electrochemical impedance spectroscopy reveals new mechanism based on competitive binding between Tris and protein on conductive biomimetic polydopamine surface.

    N. Singh, J. M. Nayak, K. Patel, S. K. Sahoo and R. Kumar, Phys. Chem. Chem. Phys., 2018, Accepted Manuscript , DOI: 10.1039/C8CP05391J

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