DataVXAIP AdvancesPaper
journal article·2016-01-01Open access

Influence of α-amylase template concentration on systematic entrapment of highly stable and monodispersed colloidal gold nanoparticles

A. Nitthin Ananth, A. Nimrodh Ananth, Sujin P. Jose, S. Umapathy, T. Mathavan

AIP Advances· Volume 6· Issue 1
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Source abstract

Abstract

Nano gold / α-amylase colloidal dispersions of profound stability were made using simple procedure with a conventional reducing agent. The surface plasmon resonance of the gold nanocrystals was used to quantify the extent of the dispersion stability and functionalization. It is found that the reduced gold nanoparticles were trapped into the protein network without denaturation the structure of α-amylase protein. This kind of entrapment of particles into the protein network prevents clustering of individual gold nanoparticles (6.42 nm ± 0.92 nm) by acting as a natural spacer. Systematic entrapment was facilitated by the affinity of gold to the sulfur moieties (Au-S) in the protein structure.
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Research context

Nanomaterials

OpenAlex topics: Gold and Silver Nanoparticles Synthesis and Applications · Protein Interaction Studies and Fluorescence Analysis · Quantum Dots Synthesis And Properties

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Madurai Kamaraj University 1 Nano Laboratory, School of Physics, , Madurai – 625 021, Tamil Nadu, India

Zhejiang University 2 MOE Key Laboratory of Macromolecular Synthesis and Functionalization, Department of Polymer Science and Engineering, , Hangzhou 310027, People’s Republic of China

Rice University 3 Department of Materials Science and Nanoengineering, , Texas 77005-1892, U.S.A.

N.M.S.S.V.N College 4 Department of Physics, , Madurai – 625 019, Tamil Nadu, India

Funding

University Grants Commission

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27. See supplementary material at http://dx.doi.org/10.1063/1.4939849 for supplementary material to this article at AIP Advances which supports the stability of α-amylase – nano gold colloidal systems and also the vibrational signature confirms that protein does not denature.