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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\u2013Visible 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\u2013Vis spectrophotometry. The stability of the proteins against heat stress was assessed by monitoring their aggregation at 48 \u00b0C, either in the presence or absence of gold nanoparticles. The gold nanoparticles were capable of suppressing the heat\u2010induced aggregation of the proteins. Furthermore, apart from possessing independent protein\u2010aggregation suppression function, the AuNPs also augmented the chaperone function of human heat shock protein 70. Findings from this study demonstrate that cyteine\u2010coated gold nanoparticles exhibit chaperone\u2010like activity and have the capability to stabilize proteins to which they may be conjugated. \u00a9 2013 IUBMB Life, 65(5):454\u2013461, 2013.<\/jats:p>","DOI":"10.1002\/iub.1146","type":"journal-article","created":{"date-parts":[[2013,2,22]],"date-time":"2013-02-22T12:06:01Z","timestamp":1361534761000},"page":"454-461","source":"Crossref","is-referenced-by-count":29,"title":["Cysteine\u2010capped gold nanoparticles suppress aggregation of proteins exposed to heat stress"],"prefix":"10.1002","volume":"65","author":[{"given":"Sifiso D.","family":"Luthuli","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Muntuwenkosi M.","family":"Chili","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neerish","family":"Revaprasadu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Addmore","family":"Shonhai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2013,2,22]]},"reference":[{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.addr.2008.03.016"},{"key":"e_1_2_7_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.matlet.2008.05.022"},{"key":"e_1_2_7_4_2","doi-asserted-by":"publisher","DOI":"10.1002\/anie.200700465"},{"key":"e_1_2_7_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0608582104"},{"key":"e_1_2_7_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cis.2007.04.021"},{"key":"e_1_2_7_7_2","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.200401335"},{"key":"e_1_2_7_8_2","doi-asserted-by":"publisher","DOI":"10.1002\/elps.200600694"},{"key":"e_1_2_7_9_2","doi-asserted-by":"publisher","DOI":"10.1002\/iub.1100"},{"key":"e_1_2_7_10_2","first-page":"665","article-title":"Molecular chaperones in biology, medicine and protein biotechnology","volume":"100","author":"Boshoff A.","year":"2004","journal-title":"South African J. 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