Probing interaction of bovine serum albumin (BSA) with the biodegradable version of cationic gemini surfactants

On the Effect of pH, Temperature, and Surfactant Structure on Bovine Serum Albumin–Cationic/Anionic/Nonionic Surfactants Interactions in Cacodylate Buffer–Fluorescence Quenching Studies Supported by UV Spectrophotometry and CD Spectroscopy

“…The observed shift and alteration in the fluorescence intensity of the attained band provide essential information about events that affect the microenvironment surrounding the aromatic residues in the protein molecule (such as protein conformational transitions, ligand binding, denaturation, etc.) [ 48 ] and may be a result of conformational changes in BSA structure, which lead to the exposure of intrinsic fluorophores to more hydrophobic environment (the change in the environment of tryptophan and an increase in hydrophobicity in the vicinity of this residue due to the presence of the alkyl chains of the surfactant molecules) [ 49 ]. On the other hand, at pH 7.4, anionic D and E residues remain near W 134 , which lies at the surface of BSA (subdomain IB) [ 50 ].…”

Milk β‐casein as delivery systems for luteolin: Multi‐spectroscopic, computer simulations, and biological studies

“…Circular Dichroism (CD) is a crucial technique commonly used for the determination of the alteration in the secondary structure of protein. The secondary structure changes of proteins after binding to ligands can be detected with far-UV CD spectroscopy (Akram et al, 2019). The amide chromophore of the peptide bonds in the et al, 2018).…”

Surfactants: physicochemical interactions with biological macromolecules

“…Another type of surfactants known as dimeric or Gemini surfactants are constructed of two monomers of surfactants which are joined by a spacer close to the hydrophilic heads (Sinha et al 2016 ). Despite their importance in several industrial fields, studies of Protein-Gemini surfactants interactions are limited, compared with those conducted with single chain surfactants (Sinha et al 2016 ; Parray et al 2018 ; Akram et al 2019 ). Several studies have revealed that some interaction mechanisms of these new generation of surfactants with proteins are shared with their corresponding monomers differing in the effects that they induce in the biomolecule, ranging from having stronger molecular interactions than their monomeric counterpart to changes or stabilization in the secondary and tertiary structures of proteins (Sinha et al 2016 ; Sonu et al 2017 ; Akram et al 2019 ).…”

“…Despite their importance in several industrial fields, studies of Protein-Gemini surfactants interactions are limited, compared with those conducted with single chain surfactants (Sinha et al 2016 ; Parray et al 2018 ; Akram et al 2019 ). Several studies have revealed that some interaction mechanisms of these new generation of surfactants with proteins are shared with their corresponding monomers differing in the effects that they induce in the biomolecule, ranging from having stronger molecular interactions than their monomeric counterpart to changes or stabilization in the secondary and tertiary structures of proteins (Sinha et al 2016 ; Sonu et al 2017 ; Akram et al 2019 ). Comparative studies of the interaction of BSA with the cationic surfactant Dodecyl Trimethyl Ammonium Bromide (DTAB) and with three Gemini-surfactants of the bis(dimethyldodecylammonium bromide) family; butanediyl-1,4-bis(dimethyldodecylammonium bromide (12–4-12,2Br −), 2-butanol-1,4-bis(dimethyldodecylammonium bromide) (12–4(OH)-12,2Br −), 2,4-dibutanol-1,4-bis(dimethyldodecylammonium bromide) (12-4(OH)2-12,2Br −), showed that at lower concentrations of the surfactant the interaction in the surfactant–protein complex is managed by electrostatic forces and while the concentration of the surfactant increases.…”

“…Sonu et al ( 2017 ) conducted a study on the effect of surfactant spacers [12-8-12, 2Br-], [12-4-12, 2Br-] and [12-4 (OH) -12, 2Br-] on the interaction with BSA and reported that the more hydrophobic the spacer is, the lower is the reduction in the number of α-helices and denaturing effects. Akram et al ( 2019 ) on the other hand, analysed the interaction of the BSA model protein with three members of a family of Gemini Cm-E20-Cm surfactants and demonstrated that the binding of these dimeric surfactants with the protein is considerably strong, without causing a significant loss of α-helix (3–4%), keeping the secondary and tertiary structure of the BSA virtually intact. Other authors have reported that the effect caused by these Gemini-surfactants on the various model proteins may be subject to changes at different temperatures, pH concentrations, ionic strength, and surfactant concentrations, among others (Faustino et al 2009 ).…”