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Influence of biological stimuli on the phase behaviour of a biomedical thermoresponsive polymer: A comparative investigation of hemeproteins

低临界溶液温度 色谱中的热响应聚合物 智能聚合物 聚合物 化学 肌红蛋白 血红素蛋白 相变 相(物质) 水溶液 生物物理学 血红素 有机化学 共聚物 生物 物理 量子力学 反相色谱法
作者
Reddicherla Umapathi,Krishan Kumar,Gokana Mohana Rani,Pannuru Venkatesu
出处
期刊:Journal of Colloid and Interface Science [Elsevier]
卷期号:541: 1-11 被引量:22
标识
DOI:10.1016/j.jcis.2019.01.062
摘要

Thorough knowledge of the biomolecular interactions between thermoresponsive polymers (TRPs) and proteins are necessary to fabricate potential materials for various bio-related science and technology applications. Although over the past four decades have evidenced that tremendous growth in the utilization of TRPs in the addition of various stimuli systems, a underlying molecular origins of the role of biological stimuli on TRPs phase transition is still missing. We demonstrated the comparative effect of heme proteins (biological stimuli) such as cytochrome c (Cyt c) and myoglobin (Mb) on the phase behaviour of poly(N-isopropylacrylamide) (PNIPAM) aqueous solution. The sophisticated multiple techniques have confirmed that the structural integrity of the proteins is found to play a vital role in altering the phase transition temperature of PNIPAM to different extents with increasing the concentration of proteins. With the addition of Cyt c, the lower critical solution temperature (LCST) of PNIPAM (33.0 °C) increased towards higher temperature (35.7 °C) in contrast to this with the addition of Mb the LCST of PNIPAM decreased towards lower temperature (30.7 °C). This discrepancy is due to the difference in contrast structural arrangements of both proteins on the LCST of PNIPAM. On the basis of these results, the variation in the structures of both heme proteins, hydration and dehydration between the heme proteins are compared. These results demonstrated that depending on the type of smart polymers used for bio-related applications, it is necessary to take into account the effect of biological stimuli while designing polymers. We hope that the present study can stimulate more novel concepts and dramatic changes in smart polymer and protein interactions.
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