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Cysteine‐capped gold nanoparticles suppress aggregation of proteins exposed to heat stress
Author(s) -
Luthuli Sifiso D.,
Chili Muntuwenkosi M.,
Revaprasadu Neerish,
Shonhai Addmore
Publication year - 2013
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1146
Subject(s) - colloidal gold , chemistry , nanoparticle , heat shock protein , sodium borohydride , bovine serum albumin , reducing agent , chaperone (clinical) , protein aggregation , biophysics , biomolecule , dynamic light scattering , cysteine , biochemistry , nanotechnology , materials science , organic chemistry , enzyme , biology , medicine , pathology , gene , catalysis
Gold nanoparticles show a lot of promise as potential agents for drug delivery and disease diagnosis. Because of this, it is important that the interaction between gold nanoparticles and biomolecules be well characterized to avoid undesirable consequences. In this study, gold nanoparticles were synthesized by the reduction of gold salt by sodium borohydride in the presence of cysteine as the capping agent. The physical features of the nanoparticles were analyzed using Ultraviolet–Visible spectrophotometry and transmission electron microscopy. The interaction between gold nanoparticles and the following proteins: bovine serum albumin, citrate synthase, malate dehydrogenase, and human heat shock protein 70 was investigated by UV–Vis spectrophotometry. The stability of the proteins against heat stress was assessed by monitoring their aggregation at 48 °C, either in the presence or absence of gold nanoparticles. The gold nanoparticles were capable of suppressing the heat‐induced aggregation of the proteins. Furthermore, apart from possessing independent protein‐aggregation suppression function, the AuNPs also augmented the chaperone function of human heat shock protein 70. Findings from this study demonstrate that cyteine‐coated gold nanoparticles exhibit chaperone‐like activity and have the capability to stabilize proteins to which they may be conjugated. © 2013 IUBMB Life, 65(5):454–461, 2013.