Exploring the Behavior of Bovine Serum Albumin in Response to Changes in the Chemical Composition of Responsive Polymers: Experimental and Simulation Studies
作者： Shih-Rong Hsieh , P. Reddy , Chi-Jung Chang , Awanish Kumar , Wan-Chi Wu
DOI: 10.3390/POLYM8060238
关键词:
摘要: Knowledge of the interactions between polymer and protein is very important to fabricate potential materials for many bio-related applications. In this regard, present work investigated effect copolymers on conformation thermal stability bovine serum albumin (BSA) with aid biophysical techniques such as fluorescence spectroscopy, circular dichroism (CD) spectroscopy differential scanning calorimetry (DSC). comparison that copolymer PGA-1.5, our results reveal PGA-1, which has a lower PEGMA/AA ratio, shows greater influence BSA. Copolymers induced unfolding polypeptide chain BSA, was confirmed from loss in negative ellipticity CD spectra. DSC showed addition PGA-1 PGA-1.5 (0.05% (w/v) decreased transition temperature by 14.8 11.5 °C, respectively). The study behavior response changes chemical composition synthetic polymers are significant various biological applications enzyme immobilization, separations, sensor development stimuli-responsive systems.
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Hideko Kanazawa, Yuki Hiruta, Yuhei Nagumo, Yuichi Suzuki, Takaaki Funatsu, Yuki Ishikawa, The effects of anionic electrolytes and human serum albumin on the LCST of poly(N-isopropylacrylamide)-based temperature-responsive copolymers. Colloids and Surfaces B: Biointerfaces. ,vol. 132, pp. 299- 304 ,(2015) , 10.1016/J.COLSURFB.2015.05.032
Shruti Mittal, Rimpy Kaur Chowhan, Laishram Rajendrakumar Singh, Macromolecular crowding: Macromolecules friend or foe Biochimica et Biophysica Acta (BBA) - General Subjects. ,vol. 1850, pp. 1822- 1831 ,(2015) , 10.1016/J.BBAGEN.2015.05.002
Burak Derkus, Kaan Cebesoy Emregul, Emel Emregul, Evaluation of protein immobilization capacity on various carbon nanotube embedded hydrogel biomaterials. Materials Science and Engineering: C. ,vol. 56, pp. 132- 140 ,(2015) , 10.1016/J.MSEC.2015.06.022
Reddicherla Umapathi, P. Madhusudhana Reddy, Awanish Kumar, Pannuru Venkatesu, Chi-Jung Chang, The biological stimuli for governing the phase transition temperature of the "smart" polymer PNIPAM in water. Colloids and Surfaces B: Biointerfaces. ,vol. 135, pp. 588- 595 ,(2015) , 10.1016/J.COLSURFB.2015.08.020
Daniel C. Carter, Joseph X. Ho, Structure of serum albumin. Advances in Protein Chemistry. ,vol. 45, pp. 153- 203 ,(1994) , 10.1016/S0065-3233(08)60640-3
W. Pfeil, P.L. Privalov, Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme denaturation by guanidine hydrochloride. Biophysical Chemistry. ,vol. 4, pp. 33- 40 ,(1976) , 10.1016/0301-4622(76)80004-X
Theodore Peters, All About Albumin: Biochemistry, Genetics, and Medical Applications ,(1995)
Pankaj Bharmoria, Arvind Kumar, Thermodynamic investigations of protein's behaviour with ionic liquids in aqueous medium studied by isothermal titration calorimetry. Biochimica et Biophysica Acta. ,vol. 1860, pp. 1017- 1025 ,(2016) , 10.1016/J.BBAGEN.2015.08.022
P. Madhusudhana Reddy, Chi-Jung Chang, Shih-Rong Hsieh, Hsin-Chun Huang, Ming-Ching Lee, Overview of the effect of monomers and green solvents on thermoresponsive copolymers: phase transition temperature and surface properties RSC Advances. ,vol. 5, pp. 86901- 86909 ,(2015) , 10.1039/C5RA18246H
Ryan J. Seelbach, Peter Fransen, Daniel Pulido, Matteo D'Este, Fabian Duttenhoefer, Sebastian Sauerbier, Thomas M. Freiman, Philipp Niemeyer, Fernando Albericio, Mauro Alini, Miriam Royo, Alvaro Mata, David Eglin, Injectable Hyaluronan Hydrogels with Peptide-Binding Dendrimers Modulate the Controlled Release of BMP-2 and TGF-β1. Macromolecular Bioscience. ,vol. 15, pp. 1035- 1044 ,(2015) , 10.1002/MABI.201500082