Hemoglobin Dynamics in Solution vis - à - vis Under Confinement - An Electrochemical Perspective
Abstract
Confining heme protein in silico often leads to beneficial functionalities such as an enhanced electrochemical response of the heme center. This can be harnessed to design effective sensors for medical diagnostics. It has been reported earlier that proteins under confinement, surface confinement on the electrode to be precise, have a more ordered and monodisperse structure compared to the protein in bulk solution. As the electrochemical response of a protein comes primarily from those protein molecules that are confined within the electrical double layer across the electrode - electrolyte interface, it is expected that restriction of conformational fluctuations of the polymeric protein will help in enhancement of the electrochemical response. This is probably the prima facie reason for electrochemical response enhancement under confinement. We examine the dynamic features of hemoglobin under confinement vis-à-vis that in bulk solution. We use a variety of spectroscopic techniques across a wide time - space window to establish the following facts: (a) hardening of the protein polypeptide backbone; (b) slowing down of protein diffusion (c) increase in relaxation times in NMR and (d) slowing down of dielectric relaxation times under confinement. This indicates an overall quenching of protein dynamics when confined inside silica matrix. From these findings, we hypothesize that along with retention of secondary structure, the quenching of dynamics contributes to the observed…
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