The identification of hydrophobic sites on the surface of proteins using absorption difference spectroscopy of bromophenol blue

Emulsifying and Foaming Properties of Protein Concentrates Prepared from Cowpea and Bambara Bean Using Different Drying Methods

“…BPB has been shown to bind to the same hydrophobic sites on proteins as fluorescent probes (12), and the absorption difference spectroscopy of BPB provides a valuable supplement to ANS for determining in solution surface hydrophobicity (11). …”

Lytic Peptides with Improved Stability and Selectivity Designed for Cancer Treatment

“…Indeed, the electrostatic attraction of peptides to cell membranes has proven to be the critical one among the three steps of peptide-membrane interactions. 23 Peptide binding to the lipid membrane was further studied on a QCM using SUVs-coated quartz crystals. There was no noticeable binding kinetics difference among peptides.…”

Application of phenol red as a marker ligand for bilirubin binding site at subdomain IIA on human serum albumin

“…The interaction of serum albumin with various dyes such as PhRed [16][17][18][19][20][21][22][23][24][25][26][27][28][29], bromophenol blue [29][30][31][32], bromocresol green [29,33], bromocresol purple [34], indocyanine green [29], sulfobromophtalein [29] and rose bengal [29,35] was studied by numerous investigators. The results obtained by Kamisaka et al [29] from the competitive binding of bilirubin and some dyes showed that the dyes compete for the common binding sites occupied by bilirubin, but the binding specificity and mode of interaction depend on the structure of the dyes and the site where the displacement occurs.…”

“…Numerous methods have been employed for studying the interaction of protein with drugs in vitro. Among those, equilibrium dialysis [47], ultrafiltration [47], spectrophotometry [34,48,49], electrophoresis [48] and chromatography [50] have been conventionally and most commonly used. In this work the binding of PhRed with HSA solution and sera in the absence and the presence of bilirubin and sulfonamides was studied using absorption and absorption difference spectroscopy.…”

“…The concentration of HSA in pH 7.4 buffer, was 8.0·10 -5 mol/L.The absorption spectroscopy may be used to identify the presence of hydrophobic site in protein with polarity-sensitive chromophores. Effect of solvent polarity on the absorption spectrum of substance can be treated as a model for the effect of binding site environment on a substance in protein[49].Fig. 4shows the absorption spectra of PhRed in isopropanolbuffer mixtures containing amounts of isopropanol from zero to 60% (v/v).…”