Abstract
We have studied the effect of biocompatible sugar based surfactant n-dodecyl β-D-maltoside (DDM) on the conformation of human serum albumin (HSA). A multi-technique approach was applied in order to understand the type of interaction and effect of DDM on the secondary and tertiary structure of HSA. Surface tension measurement showed that HSA shifted the critical micelle concentration (cmc) of the surfactant to the higher side that clarifies the complex formation between DDM and HSA which was also confirmed by UV absorption spectroscopy. Fluorescence quenching measurements showed that fluorescence of HSA was quenched by the addition of DDM with a prominent blue shift indicative of the involvement of hydrophobic interaction which was further confirmed by extrinsic fluorescence of organic dye 1-anilino-8-naphthalenesulfonate. Synchronous fluorescence measurement trends suggested that the hydrophobicity increases near the tryptophan residue while an increase in the polarity was observed near tyrosine residues. A collective information obtained by circular dicroism (CD) and Fourier-transform infra-red (FTIR) spectroscopies along with dynamic light scattering revealed the partial unfolding of the protein.