Amyloid fibrils are associated with neurodegenerative disorders and are formed by a number of proteins. In this study, the amyloid-forming behavior of several different serum albumins was examined at pH 3.5 i.e., about two pH units below their isoelectric points (pI ∼ 5.5) to examine the roles played by negative charge and hydrophobicity of exogenously added surfactants such as SDS, SDBS and AOT.

Different proteins have different amino acid sequences as well as conformations, and therefore different propensities to aggregate. Electrostatic interactions have an important role in the aggregation of proteins as revealed by our previous report (J. M. Khan et al., PLoS One, 2012, 7, e29694). In this study, we designed and executed experiments to gain knowledge of the role of charge variations on proteins during the events of protein aggregation with lysozyme as a model protein.

Role of micellar environment created by Triton X-100 (TX-100) and CHAPSO on protein conformation using IgG as a model system has been studied in this paper. A substantial amount of secondary structure with the reduction in constant tertiary contacts was obtained in both bovine and human IgG in the presence of 0.12 mM TX-100 where as 6 and 8 mM CHAPSO concentration was required for this type of secondary structure.

The effect of gelatin on the micellization behavior of amphiphilic drug nortriptyline hydrochloride (NOT) in aqueous as well as aqueous urea (250 mM) solutions has been studied using conductimetric technique. NOT is indicated for the relief of symptoms of depression. It is a tricyclic antidepressant drug. The drug interacts with gelatin similar to the interaction of surfactants and polymers. The plots of specific conductivity versusconcentration of drug were nonlinear with three different linear regions with two clear breaks.

Herein we report the interaction of amphiphilic drug clomipramine hydrochloride (CLP—a tricyclic antidepressant) with bovine serum albumin (BSA) studied by fluorescence, UV–vis, and circular dichroism (CD) spectroscopic techniques. Clomipramine hydrochloride is used to treat a variety of mental health problems. The quenching rate constant (kq) values, calculated according to the fluorescence data, decrease with increase in temperature indicating the static quenching procedure for the CLP–BSA interaction.

Herein we report the interaction of amphiphilic drug clomipramine hydrochloride (CLP—a tricyclic antidepressant) with bovine serum albumin (BSA) studied by fluorescence, UV–vis, and circular dichroism (CD) spectroscopic techniques. Clomipramine hydrochloride is used to treat a variety of mental health problems. The quenching rate constant (kq) values, calculated according to the fluorescence data, decrease with increase in temperature indicating the static quenching procedure for the CLP–BSA interaction.

The interaction of Bovine Serum Albumin (BSA) with limonene has been studied by UV-visible spectroscopy, fluorescence spectroscopy and molecular docking, and its effects on protein conformation, topology and stability were determined by Circular Dichroism (CD), Dynamic Light Scattering (DLS) and Differential Scanning Calorimetry (DSC). A gradual decrease in Stern–Volmer quenching constants with the increase in temperature showed the static mode of fluorescence quenching. The obtained binding constant (Kb) was ∼104 M−1.

In the present study the cationic gemini surfactant assisted refolding of guanidinium hydrochloride (GdCl) denatured mammalian serum albumins viz. sheep serum albumin (SSA), rat serum albumin (RSA) and porcine serum albumin (PSA) using a combination of cationic gemini surfactants, pentanediyl-α,ω-bis(cetyldimethylammonium bromide) (C16H33(CH3)2N+–(CH2)5–N+(CH3)2C16H33)⋅2Br− designated as G5 and methyl-β-cyclodextrin in the artificial chaperone assisted two step method, is attempted.

Amyloid fibril formation by proteins leads to variety of degenerative disorders called amyloidosis. While these disorders are topic of extensive research, effective treatments are still unavailable. Thus in present study, two anti-tuberculosis drugs, i.e., pyrazinamide (PYZ) and D-cycloserine (DCS), also known for treatment for Alzheimer’s dementia, were checked for the anti-aggregation and anti-amyloidogenic ability on Aβ-42 peptide and hen egg white lysozyme.

In this work, we investigated the inhibitory ability of taurine on the aggregation of Human serum albumin (HSA) and also examined how it controls the kinetic parameters of the aggregation process. We demonstrated the structural alterations in the HSA after binding to the taurine at 65 °C by exploiting various biophysical techniques. UV–vis spectroscopy was used to check the turbidometric changes in the protein. Thioflavin T fluorescence kinetics was subjected to explore kinetic parameters comparing the amyloid formation in the presence of varying concentration of taurine.