Interaction of triprolidine hydrochloride with serum albumins: Thermodynamic and binding characteristics, and influence of site probes

Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes

“…H > 0 and S > 0 alludes a hydrophobic interaction [37]; H < 0 and S < 0 suggests the van der Waals force or hydrogen bond formation [38]; and H < 0 and S > 0 reflects an electrostatic force [39]. Besides, the negative values of G reveals that the binding process was spontaneous [22,40].…”

Biophysical characterization of the interaction between human serum albumin and n-dodecyl β-d-maltoside: A multi-technique approach

“…Amide I band originates between 1600 and 1700 cm −1 and is due to the C O stretching while amide II band appears in between 1500 and 1600 cm −1 owing to the C N stretching coupled with N H bending [52,53]. The amide I band is considered as more sensitive for understanding the changes in the secondary structures of proteins [54,55] and the ␣-helical contents of the proteins give the particular absorption at wavelengths which are ranging from 1652 to 1662 cm −1 [56,57]. Therefore, the peak at 1650 cm −1 detected for native HSA is ascribed to the ␣-helix of HSA (Fig.…”

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

“…BSA shows 76 % similarity with that of HSA [3], which has a single-chain with 582 amino acid residues. Moreover, it has two tryptophan residues (Trp134 and Trp212), that is to say, Trp-134 in the first domain is located on the surface of the molecule, and Trp-212 in the second domain is located within a hydrophobic binding pocket of BSA, whereas, HSA consists of a single polypeptide chain with 585 amino acid residues in which the single tryptophan residue (Trp214) measures the drug-binding affinity [4,5]. For many years, the interactions between SAs and small molecular probes have attracted a great deal of interest due to their application in a great variety of biological, pharmaceutical, toxicological and cosmetic systems [6].…”