Determination of hydrophobicity of albumins and other proteins using a near-infrared probe

✍ Scribed by Miquel D. Antoine; Shrinivasan Devanathan; Gabor Patonay

• Publisher: Elsevier Science
• Year: 1991
• Tongue: English
• Weight: 678 KB
• Volume: 47
• Category: Article
• ISSN: 1386-1425
• DOI: 10.1016/0584-8539(91)80128-6

✦ Synopsis

Near-infrared spectroscopy (NIR) is used to investigate the hydrophobicity of binding sites on mammalian serum albumins. The binding sites on albumins are probed using an NIR dye which showed signficant changes in its NIR absorption spectra depending on the hydrophobicity of solvent in an earlier study. The notable differences observed in the NIR spectra of this dye indicate that the hydrophobicity of the microenvironment around the binding site may be determined using this probe. The absorption spectra of this NIR dye show two distinct maxima dependent upon the hydrophobicity of the environment. The intensity of these peaks was used for determining hydrophobicity. The hydrophobicity of the binding site was also evaluated by small additions of isopropyl alcohol to change the bulk solvent hydrophobicity. NIR measurements confirm that the microenvironment of the dye binding area is relatively hydrophobic. This NIR method is suitable for the determination of the hydrophobicity of soluble proteins.