Protein carries out its biological activities in the extremely crowded environment inside the cell.1 There is a growing interest of this crowding effect on the biological processes like protein folding, gene expression and conformational transition of macromolecules.2 Recently, liquid-liquid phase separation has gained much interests to the scientific community because of its different dynamical nature compared to the less crowded bulk phase.3 Complex crowded environment generates membrane less organelles through the liquid-liquid phase separation and regulates different dynamics of the biomolecules compared to the bulk phase. Here, we have studied the structure, dynamics and activity of a plasma protein called Human Serum Albumin (HSA) inside a pluoronic triblock copolymer gel (F127).4 CD spectra reveal that the protein occupies more stable structure inside the F127 gel compared to that of the bulk. This phenomenon is also substantiated by the esterase activity assay of the protein both in F127 gel and bulk. FCS data explain the retardation of the conformational dynamics of the protein inside F127 gel. The fast component is slowed down by ~55 times and the slow component by ~20 times. FCS data also conclude that translational diffusion of the protein is 59 times slower inside the F127 gel compared to the bulk water. In contrast to that, rotational relaxation time shows almost similar result both F127 gel and in buffer. CPM labelled HSA shows a slight faster solvation dynamic inside the F127 (𝜏S = 300 ps) with respect to the bulk water (𝜏S = 600 ps). This can be ascribed that solvation and rotational dynamics are controlled mostly by the immediate environment of the probe which is almost same both in gel and buffer. Modulation of FRET efficiency between two covalently linked fluorophore in the crowded environment also ensures the change in the distance between two domains of HSA. This study helps us to understand the fundamental dynamical nature of HSA in the crowded environment.

Effect of Crowding Environment on Protein’s Structure Along with Its Regulation on Protein Dynamical Behavior.

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27th CRSI National Symposium in Chemistry

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