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pH-Dependent Protein Conformational Changes in Albumin:Gold Nanoparticle Bioconjugates: A Spectroscopic Study

Shang, Li, Wang, Yizhe, Jiang, Junguang, Dong, Shaojun·2007·Langmuir

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.

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Metadata

Authors
Shang, L., Wang, Y., Jiang, J., & Dong, S.
Venue
Langmuir
Published
2007-01-24
Volume
23
Issue
5
Pages
2714-2721
ISSN
  • 0743-7463 (ISSN-L)
  • 1520-5827
OpenAlex
W1990379353
Cited by
557
References
0
FWCI
6.70
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: pH-Dependent Protein Conformational Changes in Albumin:Gold Nanoparticle Bioconjugates: A Spectroscopic Study. https://app.cochat.ai/papers/10.1021/la062064e
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Shang, L., Wang, Y., Jiang, J., & Dong, S. (2007). pH-Dependent Protein Conformational Changes in Albumin:Gold Nanoparticle Bioconjugates: A Spectroscopic Study. Langmuir. https://doi.org/10.1021/la062064e

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