Spectroscopic studies on the interaction of cationic surfactants with bovine serum albumin

Study of nobiletin binding to bovine serum albumin by capillary electrophoresis–frontal analysis and circular dichroism

“…4, we can see that the spectrum of BSA consists of two peaks, centered at 208 and 222 nm. Peaks at 208 and 222 nm are characteristic of the α-helix (Gull et al, 2009). The CD spectra of BSA in the presence and absence of NOB were similar in shape, indicating that the structure of BSA was still predominantly α-helix (Zhang et al, 2009).…”

Amino acid-based cationic gemini surfactant–protein interactions

“…Fluorescence of BSA is usually dominated by the contribution of its aromatic amino acid residues, namely tyrosine (Tyr), tryptophan (Trp) and phenylalanine (Phe), the emission of the latter one being negligible in most cases [26][27][28]50,57]. The variations in the fluorescence spectra obtained by exciting the protein at 295 nm have been attributed to the presence of tryptophan residues while the changes that result from protein excitation at 280 nm are associated with both tryptophan and tyrosine residues [26,28].…”

“…The variations in the fluorescence spectra obtained by exciting the protein at 295 nm have been attributed to the presence of tryptophan residues while the changes that result from protein excitation at 280 nm are associated with both tryptophan and tyrosine residues [26,28]. As the fluorescence intensity and the wavelength of emission maximum ( max ) are sensitive to protein conformation, these parameters become important tools in probing protein folding and/or unfolding processes [20][21][22][23]50,57]. BSA has 19 Tyr residues in different domains and two Trp residues, namely Trp 134, present at the protein surface in domain I, and Trp 213, present in the hydrophobic binding pocket of the protein in domain II, that act as intrinsic fluorophores [58,59].…”

Exploring the Protein Stability Landscape: Bacillus subtilis Lipase A as a Model for Detergent Tolerance

“…[9] Cationic detergents are considered less destabilizing because they form fewer electrostatic interactions at neutral pH; instead, destabilization is most likely the result of interactions with the hydrophobic tail. [10][11][12] Zwitterionic detergents combine both types of charge over a broad pH range. [13] Nonionic detergents exhibit comparatively weak protein interactions.…”