Distinct interactional behaviour of an ecofriendly cleavable gemini surfactant with myoglobin: physicochemical and spectroscopic study.

Protein-surfactant interactions are substantial to industrial and cosmetic compilations. In this regard, we have studied the interaction of cleavable gemini surfactant (C16-C4O2-C16) with the myoglobin (Mb), utilizing physicochemical and spectroscopic approach. The results obtained were quite intriguing. Tensiometry has shown that pure C16-C4O2-C16 bear lower surface tension (γ) and CMC values than mixed systems (C16-C4O2-C16 + Mb). Intrinsic fluorescence results showed enhancement in the fluorescence intensity upon cleavable gemini binding. UV results depict visible fluctuations in the peaks corresponding to π-π* transitions, Soret band and Q-bands. CD spectra advocate the unfolding of myoglobin polypeptide networking upon C16-C4O2-C16 intercalation. Significant decrement in the α-helicity infers the rapture of native myoglobin into denatured state. 1HNMR results delineated unfolding owing to significant change in chemical shift values and peak disappearances/broadening. FT-IR peak shift describes unfolding of Mb. Finally, docking gives a clear view of localization of cleavable surfactant into the hydrophobic domains of Mb. Docking interaction energy depicts feasibility of C16-C4O2-C16 and Mb interaction.