Serum albumins are chief carrier of ligands in blood, hence important in clinical biotechnology. The effects of methyl cyanide (MeCN), a chief solvent of reverse phase chromatography, on four mammalian serum albumins (human, bovine, porcine and rabbit sources) were studied at neutral pH with the help of scattering, circular dichroism, IR and fluorescence spectroscopy. We have detected an intermediate state in the presence of 20% (v/v) MeCN, having 8–9% higher α-helical structure than that of their native states.

The interaction of bovine serum albumin (BSA) with cetyltrimethylammonium bromide (CTAB), C16C4C16Br2, Brij58, and their binary mixtures has been studied using tensiometry, spectrofluorometry, and circular dichroism at physiological pH and 25 °C. The tensiometric profiles of CTAB and C16C4C16Br2 in the presence of BSA exhibit a single break at a lower surfactant concentration termed as C1 (concentration corresponding to saturation of the interface) compared to their critical micelle concentration (CMC) in the buffered solution.

This is the first report of its kind that well demonstrates that a lectin from Phytolacca americana[Pa-2 (P. americana lectin-2)] can also be intrinsically unordered, based on the results obtained by CD, tryptophan fluorescence, ANS (8-anilinonaphthalene-1-sulfonic acid) binding, acrylamide quenching, DLS (dynamic light scattering) and its amino acid composition database analyses. Pa-2 is an acidic monomeric lectin and acquires random coil conformation at neutral pH without any regular secondary structure.

The interactions of bovine serum albumin (BSA) with cationic gemini surfactants alkanediyl-α,ω-bis(dimethylcetylammonium bromide) (designated as C16CsC16Br2,s = 4, 5, and 6) and single chain surfactant cetyltrimethylammonium bromide (CTAB) have been investigated with tensiometry, Rayleigh's scattering, fluorescence spectroscopy, and circular dichroism at physiological pH and 25 °C.

Effect of cationic surfactant, cetyltrimethylammonium bromide (CTAB) addition on the thermal denaturation of rabbit serum albumin (RSA) has been studied by employing small-angle neutron scattering (SANS), circular dichroism (CD), intrinsic fluorescence and ultra violet (UV) spectroscopy. The studies were performed at three different temperatures viz., 30, 50 and 70 °C and at two different concentrations of CTAB: the low concentration of CTAB used was 1 mM and the higher concentration was 80 mM (for SANS) and 20 mM (for CD, fluorescence and UV).

Unfolding of rabbit serum albumin (RSA) by cationic surfactants cetyltrimethylammonium bromide (CTAB) and tetradecyltrimethylammonium bromide (TTAB) was studied by exploiting surface tensiometry, small-angle neutron scattering (SANS), intrinsic fluorescence, resonance Rayleigh scattering (RRS) (also referred as turbidity at 350/350), and circular dichroism (CD) techniques. Surface tension measurements revealed the formation of highly surface-active complexes occurring as a consequence of RSA–surfactants interactions.

Herein we report our studies carried out on the interaction between IMP and gelatin in aqueous medium at 25 °C using conductimetry, surface tensiometry and circular dichroism (CD) techniques. Both surface tensiometry and conductimetry results indicate that the drug interacts with the gelatin in a surfactant-like manner, i.e., both critical aggregation (cac) and polymer saturation points (psp) were observed. The interaction starts with the formation of a highly surface-active complex as revealed by the lowering of surface tension on the addition of drug to the macromolecule.

The interaction of the amphiphilic drugs, i.e., amitriptyline hydrochloride (AMT) and promethazine hydrochloride (PMT), with serum albumins (i.e., human serum albumin (HSA) and bovine serum albumin (BSA)), has been examined by the various spectroscopic techniques, like fluorescence, UV–vis, and circular dichroism (CD).

Surfactants prevent the irreversible aggregation of partially refolded proteins, and they are also known to assist in protein refolding. A novel approach to protein refolding that utilizes a pair of low molecular weight folding assistants, a detergent and cyclodextrin, was proposed by Rozema and Gellman (D. Rozema, S.H. Gellman, J. Am. Chem. Soc. 117 (1995) 2373). We report the refolding of bovine serum albumin (BSA) assisted by these artificial chaperones, utilizing gemini surfactants for the first time.