pH-Dependent Protein Conformational Changes in Albumin:Gold Nanoparticle Bioconjugates: A Spectroscopic Study
Citations Over TimeTop 10% of 2007 papers
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.
Related Papers
- → Structural Changes of β-Lactoglobulin during Thermal Unfolding and Refolding – An FT-IR and Circular Dichroism Study(2005)90 cited
- → Feasibility of circular dichroism to study protein structure at extreme concentrations(2019)28 cited
- → Study of the Interaction between Bovine Serum Albumin and Ligustrazine with Spectroscopic Techniques(2013)2 cited
- Circular Dichroism Spectra and Secondary Structures in Solution of Flammulin(2000)
- [Analysis of the secondary structure of urokinase by the circular dichroism method].(1984)