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Issue 21, 2016
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Startling temperature effect on proteins when confined: single molecular level behaviour of human serum albumin in a reverse micelle

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Abstract

The present work reports the effect of confinement, and temperature therein, on the conformational fluctuation dynamics of domain-I of human serum albumin (HSA) by fluorescence correlation spectroscopy (FCS). The water-pool of a sodium bis(2-ethylhexyl)sulfosuccinate (AOT) reverse micelle has been used as the confined environment. It was observed that the conformational fluctuation time is about 6 times smaller compared to bulk medium when confined in a water-pool of 3.5 nm radius. On increasing the size of the water-pool the conformational fluctuation time was found to increase monotonically and approaches the bulk value. The effect of confinement is on par with the general belief about the restricted motion of a macromolecule upon confinement. However, the effect of temperature was found to be surprising. An increase in the temperature from 298 K to 313 K induces a larger change in the conformational fluctuation time in HSA, when confined. In the bulk medium, apparently there is no change in the conformational fluctuation time in the aforementioned temperature range, whereas, when HSA is present in an AOT water-pool of radius 3.5 nm, about an 88% increase in the fluctuation time was observed. The observed prominent thermal effect on the conformational dynamics of domain-I of HSA in the water-pool of an AOT reverse micelle as compared to in the bulk medium was concluded to arise from the confined solvent effect.

Graphical abstract: Startling temperature effect on proteins when confined: single molecular level behaviour of human serum albumin in a reverse micelle

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Publication details

The article was received on 21 Jan 2016, accepted on 16 Apr 2016 and first published on 22 Apr 2016


Article type: Paper
DOI: 10.1039/C6CP00452K
Phys. Chem. Chem. Phys., 2016,18, 14350-14358
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    Startling temperature effect on proteins when confined: single molecular level behaviour of human serum albumin in a reverse micelle

    B. Sengupta, R. Yadav and P. Sen, Phys. Chem. Chem. Phys., 2016, 18, 14350
    DOI: 10.1039/C6CP00452K

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