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  • Title: Interaction of myoglobin with poly(methacrylic acid) at different pH in their layer-by-layer assembly films: an electrochemical study.
    Author: Guo W, Hu N.
    Journal: Biophys Chem; 2007 Sep; 129(2-3):163-71. PubMed ID: 17566631.
    Abstract:
    Myoglobin (Mb), with net positive surface charges at pH 5.0, was successfully assembled into layer-by-layer films on various solid surfaces with poly(methacrylic acid) (PMAA) at different pH, designated as {PMAA(pH 5.0)/Mb}n, {PMAA(pH 6.5)/Mb}n, and {PMAA(pH 8.0)/Mb}n, respectively. As a weak polycarboxylic acid with pKa=6 - 7, PMAA carried different negative charges at different pH due to different ionization degree of its carboxylic acid groups. Quartz crystal microbalance (QCM), UV-vis spectroscopy, and cyclic voltammetry (CV) were used to monitor and confirm the assembly of {PMAA/Mb}n films. All the results showed that the adsorption amount of Mb in each bilayer had an "unexpected" sequence of {PMAA(pH 5.0)/Mb}n>{PMAA(pH 6.5)/Mb}n>{PMAA(pH 8.0)/Mb}n, which could be explained by the formation of soluble complex of PMAA-Mb at pH 8.0 and the cooperative effect of hydrogen bonding and induced electrostatic interaction between Mb and PMAA at pH 5.0. The influence of ionic strength in exposure solution and in Mb adsorbate solution was investigated, and the results supported the above explanations. The {PMAA/Mb}n films provided a suitable microenvironment for Mb to retain its near-native structure and transfer electron with underlying electrodes. The reversible CV peak pair for Mb Fe(III)/Fe(II) redox couple could be used to catalyze reduction of hydrogen peroxide electrochemically, showing the potential applicability of the films as the new type of biosensors or bioreactors based on the direct electrochemistry of Mb. The electrochemical and electrocatalytic behaviors of protein layer-by-layer films with weak polyelectrolytes could thus be controlled by adjusting the solution pH of weak polyelectrolytes.
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