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Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin

The interaction of gold nanoparticles, synthesized using Curcuma mangga extract (CM-AuNPs) with human serum albumin (HSA) was investigated with the help of fluorescence, UV absorption and circular dichroism (CD) spectroscopy. In view of the positive correlation of Stern-Volmer constant with temperat...

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Main Authors: Foo, Yiing Yee, Kabir, Md Zahirul, Periasamy, Vengadesh, Malek, Sri Nurestri Abd, Tayyab, Saad
Format: Article
Published: Elsevier 2018
Subjects:
Q Science (General)
QC Physics
QH Natural history
Online Access:http://eprints.um.edu.my/22064/
https://doi.org/10.1016/j.molliq.2018.05.115
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spelling my.um.eprints.220642019-08-26T03:55:09Z http://eprints.um.edu.my/22064/ Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin Foo, Yiing Yee Kabir, Md Zahirul Periasamy, Vengadesh Malek, Sri Nurestri Abd Tayyab, Saad Q Science (General) QC Physics QH Natural history The interaction of gold nanoparticles, synthesized using Curcuma mangga extract (CM-AuNPs) with human serum albumin (HSA) was investigated with the help of fluorescence, UV absorption and circular dichroism (CD) spectroscopy. In view of the positive correlation of Stern-Volmer constant with temperature, quenching of protein fluorescence observed upon addition of CM-AuNPs seems to occur through collisional mechanism. The quenching mechanism was further substantiated by UV absorption spectral results, where no significant change in the absorption spectrum of HSA was observed upon addition of CM-AuNPs. Analysis of the fluorescence quenching titration data revealed moderate binding affinity (Ka = 0.97 × 104 M−1 at 298 K) between CM-AuNP and HSA. The complexation between CM-AuNP and HSA was predicted to be stabilized by hydrophobic forces, as reflected from the thermodynamic data (ΔH = +35.5 kJ mol−1 and ΔS = +195.62 J mol−1 K−1). Three-dimensional fluorescence spectral analysis demonstrated perturbation of microenvironment around Trp and Tyr residues in HSA upon CM-AuNPs addition. While interaction between CM-AuNP and HSA produced significant tertiary structural change in the protein, secondary structures remained unaltered, as elucidated by near-UV and far-UV CD spectral analyses, respectively. ANS displacement experiments suggested Sudlow's Site II, located in subdomain IIIA, as the preferred binding site of CM-AuNP on HSA. Elsevier 2018 Article PeerReviewed Foo, Yiing Yee and Kabir, Md Zahirul and Periasamy, Vengadesh and Malek, Sri Nurestri Abd and Tayyab, Saad (2018) Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin. Journal of Molecular Liquids, 265. pp. 105-113. ISSN 0167-7322 https://doi.org/10.1016/j.molliq.2018.05.115 doi:10.1016/j.molliq.2018.05.115
institution Universiti Malaya
building UM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaya
content_source UM Research Repository
url_provider http://eprints.um.edu.my/
topic Q Science (General)
QC Physics
QH Natural history
spellingShingle Q Science (General)
QC Physics
QH Natural history
Foo, Yiing Yee
Kabir, Md Zahirul
Periasamy, Vengadesh
Malek, Sri Nurestri Abd
Tayyab, Saad
Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin
description The interaction of gold nanoparticles, synthesized using Curcuma mangga extract (CM-AuNPs) with human serum albumin (HSA) was investigated with the help of fluorescence, UV absorption and circular dichroism (CD) spectroscopy. In view of the positive correlation of Stern-Volmer constant with temperature, quenching of protein fluorescence observed upon addition of CM-AuNPs seems to occur through collisional mechanism. The quenching mechanism was further substantiated by UV absorption spectral results, where no significant change in the absorption spectrum of HSA was observed upon addition of CM-AuNPs. Analysis of the fluorescence quenching titration data revealed moderate binding affinity (Ka = 0.97 × 104 M−1 at 298 K) between CM-AuNP and HSA. The complexation between CM-AuNP and HSA was predicted to be stabilized by hydrophobic forces, as reflected from the thermodynamic data (ΔH = +35.5 kJ mol−1 and ΔS = +195.62 J mol−1 K−1). Three-dimensional fluorescence spectral analysis demonstrated perturbation of microenvironment around Trp and Tyr residues in HSA upon CM-AuNPs addition. While interaction between CM-AuNP and HSA produced significant tertiary structural change in the protein, secondary structures remained unaltered, as elucidated by near-UV and far-UV CD spectral analyses, respectively. ANS displacement experiments suggested Sudlow's Site II, located in subdomain IIIA, as the preferred binding site of CM-AuNP on HSA.
format Article
author Foo, Yiing Yee
Kabir, Md Zahirul
Periasamy, Vengadesh
Malek, Sri Nurestri Abd
Tayyab, Saad
author_facet Foo, Yiing Yee
Kabir, Md Zahirul
Periasamy, Vengadesh
Malek, Sri Nurestri Abd
Tayyab, Saad
author_sort Foo, Yiing Yee
title Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin
title_short Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin
title_full Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin
title_fullStr Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin
title_full_unstemmed Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin
title_sort spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin
publisher Elsevier
publishDate 2018
url http://eprints.um.edu.my/22064/
https://doi.org/10.1016/j.molliq.2018.05.115
_version_ 1643691741940809728
score 13.211869

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