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| - Interactions between Bovine β-Lactoglobulin A and VariousBioactive Peptides As Studied by Front-Face FluorescenceSpectroscopy
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| - Front-face fluorescence spectroscopy was used for the first time to study the interactions betweenbovine β-lactoglobulin variant A (β-Lg A) and various β-Lg-derived bioactive peptides. Fluorescencespectra were recorded for β-Lg A-peptide mixtures at 25 °C and pH 6.8 with an excitation wavelengthof 290 nm to characterize the molecular environment of tryptophan (Trp) residues present in theprotein but absent in the peptides. Spectra remained unchanged following addition of peptides β-Lgf92−100 and β-Lg f125−135, while Phe−Phe interaction between β-Lg f69−83 molecules interferedwith analysis. Addition of β-Lg f102−105 produced a blue shift (3 nm) and a significant increase influorescence intensity, while addition of β-Lg f142−148 also caused a significant increase influorescence intensity but accompanied by a red shift (3 nm). These results indicate that the polarityof the Trp environment in the β-Lg A structure may be modified differently depending on the peptideadded. Keywords: Bovine β-lactoglobulin A; bioactive peptide; front-face fluorescence spectroscopy; protein−peptide interaction.
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