Translator Disclaimer
1 November 2005 Vibrational Spectroscopic Studies on the Disulfide Formation and Secondary Conformational Changes of Captopril–HSA Mixture after UV-B Irradiation
Author Affiliations +
Abstract

The effects of pH and ultraviolet-B (UV-B) irradiation on the secondary structure of human serum albumin (HSA) in the absence or presence of captopril were investigated by an attenuated total reflection (ATR)/Fourier transform infrared (FTIR) spectroscopy. The UV-B exposure affecting the stability of captopril before and after captopril–HSA interaction was also examined by using confocal Raman microspectroscopy. The results indicate that the transparent pale-yellow solution for captopril–HSA mixture in all pH buffer solutions, except pH 5.0∼7.0, changed into a viscous form then a gel form with UV-B exposure time. The secondary structural transformation of HSA in the captopril–HSA mixture with or without UV-B irradiation was found to shift the maxima amide I peak in IR spectra from 1652 cm−1 assigned to α-helix structure to 1622 cm−1 because of a β-sheet structure, which was more evident in pH 3.0, 8.0 or 9.0 buffer solutions. The Raman shift from 1653 cm−1 (α-helix) to 1670 cm−1 (β-sheet) also confirmed this result. Captopril dissolved in distilled water with or without UV-B irradiation was determined to form a captopril disulfide observed from the Raman spectra of 512 cm−1, which was exacerbated by UV-B irradiation. There was little disulfide formation in the captopril–HSA mixture even with long-term UV-B exposure, but captopril might interact with HSA to change the protein secondary structure of HSA whether there was UV-B irradiation or not. The pH of the buffer solution and captopril–HSA interaction may play more important roles in transforming the secondary structure of HSA from α-helix to β-sheet in the corresponding captopril–HSA mixture than UV-B exposure. The present study also implies that HSA has the capability to protect the instability of captopril in the course of UV-B irradiation. In addition, a partial unfolding of HSA induced by pH or captopril-HSA interaction under UV-B exposure is proposed.

Mei-Jane Li and Shan-Yang Lin "Vibrational Spectroscopic Studies on the Disulfide Formation and Secondary Conformational Changes of Captopril–HSA Mixture after UV-B Irradiation," Photochemistry and Photobiology 81(6), 1404-1410, (1 November 2005). https://doi.org/10.1562/2005-04-25-RN-497
Received: 25 April 2005; Accepted: 1 June 2005; Published: 1 November 2005
JOURNAL ARTICLE
7 PAGES

This article is only available to subscribers.
It is not available for individual sale.
+ SAVE TO MY LIBRARY

SHARE
ARTICLE IMPACT
RIGHTS & PERMISSIONS
Get copyright permission
Back to Top