1. pH-Dependent Protein Conformational Changes in Albumin:Gold Nanoparticle Bioconjugates: A Spectroscopic Study
- Author
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Shaojun Dong, Yizhe Wang, Junguang Jiang, and Li Shang
- Subjects
Circular dichroism ,Protein Conformation ,Molecular Conformation ,Analytical chemistry ,Serum albumin ,Metal Nanoparticles ,Infrared spectroscopy ,Photochemistry ,Protein structure ,Albumins ,Spectroscopy, Fourier Transform Infrared ,Electrochemistry ,Animals ,General Materials Science ,Bovine serum albumin ,skin and connective tissue diseases ,Protein secondary structure ,Spectroscopy ,biology ,Chemistry ,Circular Dichroism ,Serum Albumin, Bovine ,Surfaces and Interfaces ,Hydrogen-Ion Concentration ,Condensed Matter Physics ,Protein tertiary structure ,Spectrometry, Fluorescence ,Models, Chemical ,Spectrophotometry ,Colloidal gold ,biology.protein ,Cattle ,Spectrophotometry, Ultraviolet ,Gold ,sense organs - Abstract
The conformational changes of bovine serum albumin (BSA) in the albumin:gold nanoparticle bioconjugates were investigated in detail by various spectroscopic techniques including UV-vis absorption, fluorescence, circular dichroism, and Fourier transform infrared spectroscopies. Our studies suggested that albumin in the bioconjugates that was prepared by the common adsorption method underwent substantial conformational changes at both secondary and tertiary structure levels. BSA was found to adopt a more flexible conformational state on the boundary surface of gold nanoparticles as a result of the conformational changes in the bioconjugates. The conformational changes at pH 3.8, 7.0, and 9.0, which corresponded to different isomeric forms of albumin, were investigated, respectively, to probe the pH effect on the conformational changes of BSA in the bioconjugates. The results showed that the pH of the medium influenced the changes greatly and that fluorescence and circular dichroism studies further indicated that the changes were larger at higher pH.
- Published
- 2007
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