Some aspects of β-lactoglobulin structural properties in solution studied by fluorescence quenching

Comparative analysis of refolding of chemically denatured β-lactoglobulin types A and B using the dilution additive mode

“…From the Papiz et al crystal structure [31], Trp19 is at the base of the central hydrophobic calyx of the protein, while Trp61 is part of an external loop. The intrinsic fluorescence of BLG is then almost exclusively attributed to Trp19, positioned in a more apolar environment than Trp61 [8]. Fig.…”

“…BLG is part of the lipocalin superfamily of hydrophobic molecule transporters [8]. The interaction of BLG with a great variety of hydrophobic ligands, such as retinal, fatty acids, triglycrides, hemin, ellipticine (antitumor drug), aromatic hydrocarbons and carcinogenic hydrocarbons [9,10].…”

Characterization of resveratrol–milk protein interaction

“…Concerning BLG, a larger polarity is reported to be consequence of disruption of the protein tertiary structure with the exposure of a fluorophore originally sited in an apolar environment. As hypothesized for riboflavin, the binding can induce a slight opening of the hydrophobic cavity exposing the Trp-19 sited Table 1 Zeta potential (mv) of proteins solutions alone (5, 10, 20, 40 and 80 lM) resveratrol solutions (5, 10, 15, 20, 40 and 80 lM) at the bottom of the pocket to a more hydrophilic environment (Busti et al, 1998;Diarrassouba et al, 2013). Beyond a critical concentration of resveratrol the quenching events reached a maximum, indicating that the accessible fluorophores are completely quenched.…”

Spectroscopic and cytotoxic studies of the novel designed palladium(II) complexes: β-Lactoglobulin and K562 as the targets

“…From the crystal structure studies [27], Trp19 is at the base of the central hydrophobic calyx of the protein, while Trp61 is part of an external loop. The intrinsic fluorescence of BLG is then almost exclusively attributed to Trp19, positioned in a more apolar environment than Trp61 [28]. of dithiocarbamate moiety of the ligands on the BLG tertiary structure is much greater than difference in the alkyl side chain of these complexes.…”