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Polymers 2016, 8(6), 238; doi:10.3390/polym8060238

Exploring the Behavior of Bovine Serum Albumin in Response to Changes in the Chemical Composition of Responsive Polymers: Experimental and Simulation Studies

1
Department of Surgery, Taichung Veterans General Hospital, 1650 Taiwan Boulevard Section 4, Taichung 40705, Taiwan
2
Department of Chemical Engineering, Feng Chia University, 100, Wenhwa Road, Seatwen, Taichung 40724, Taiwan
3
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
4
School of Pharmacy, China Medical University, 91, Hsueh-Shih Road, Taichung 40402, Taiwan
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Martin Kröger
Received: 3 May 2016 / Revised: 13 June 2016 / Accepted: 13 June 2016 / Published: 18 June 2016
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Abstract

Knowledge of the interactions between polymer and protein is very important to fabricate the potential materials for many bio-related applications. In this regard, the present work investigated the effect of copolymers on the conformation and thermal stability of bovine serum albumin (BSA) with the aid of biophysical techniques such as fluorescence spectroscopy, circular dichroism (CD) spectroscopy and differential scanning calorimetry (DSC). In comparison with that of copolymer PGA-1.5, our fluorescence spectroscopy results reveal that the copolymer PGA-1, which has a lower PEGMA/AA ratio, shows greater influence on the conformation of BSA. Copolymers induced unfolding of the polypeptide chain of BSA, which was confirmed from the loss in the negative ellipticity of CD spectra. DSC results showed that the addition of PGA-1 and PGA-1.5 (0.05% (w/v) decreased the transition temperature by 14.8 and 11.5 °C, respectively). The results from the present study on the behavior of protein in response to changes in the chemical composition of synthetic polymers are significant for various biological applications such as enzyme immobilization, protein separations, sensor development and stimuli-responsive systems. View Full-Text
Keywords: protein; responsive polymer; thermal stability; folding; unfolding; biomedical applications protein; responsive polymer; thermal stability; folding; unfolding; biomedical applications
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Hsieh, S.-R.; Reddy, P.M.; Chang, C.-J.; Kumar, A.; Wu, W.-C.; Lin, H.-Y. Exploring the Behavior of Bovine Serum Albumin in Response to Changes in the Chemical Composition of Responsive Polymers: Experimental and Simulation Studies. Polymers 2016, 8, 238.

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