alexa Investigation of Ph-Assisted Human Serum Albumin (HSA)-
ISSN: 2157-7439

Journal of Nanomedicine & Nanotechnology
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Research Article

Investigation of Ph-Assisted Human Serum Albumin (HSA)-Cobalt (Co)Binding Using Nanomechanical Deflection and Circular Dichroism

Garima Thakur1*, Seonghwan Kim1,2, Kovur Prashanthi1 and Thomas Thundat1

1Department of Chemical and Materials Engineering, University of Alberta, Edmonton, AB, T6G 2V4, Canada

2Department of Mechanical and Manufacturing Engineering, University of Calgary, Calgary, AB, T6G 2V4, Canada

*Corresponding Author:
Garima Thakur
Department of Chemical and Materials Engineering
University of Alberta, Edmonton, AB, T6G 2V4, Canada
Tel: 780-492-8664
E-mail: [email protected]

Received Date: December 19, 2013; Accepted Date: February 21, 2014; Published Date: February 24, 2014

Citation: Thakur G, Kim S, Prashanthi K, Thundat T (2014) Investigation of Ph-Assisted Human Serum Albumin (HSA)-Cobalt (Co) Binding Using Nanomechanical Deflection and Circular Dichroism. J Nanomed Nanotechol S5:008. doi:10.4172/2157-7439.S5-008

Copyright: © 2014 Thakur G, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.



Human serum albumin (HSA)-cobalt (Co) binding assay could assist in early detection of myocardial ischemia.
However, the binding mechanism of the HSA-Co assay is very complex and hard to detect. During myocardial
ischemia, the physiological pH may change with subsequent decrease in binding of Co with HSA. In this paper, we have investigated the binding of Co with HSA functionalized on the surface of microcantilever at an acidic, basic and neutral pH. Conformational change of HSA upon injection of Co(II) ions as analyteat various pH, resulted in nanomechanical deflection of cantilevers. Furthermore, spectroscopic insight was obtained using circular dichroism to analyze conformational change of HSA-Co(II) binding.


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