LAUSR

HYPOTHESIS 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. EXPERIMENTS 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. FINDINGS 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.