Colorimetric detection of lysozyme based on electrostatic interaction with human serum albumin-modified gold nanoparticles.
In this study, an aqueous solution of 13-nm gold nanoparticles (AuNPs) covalently bonded with human serum albumin (HSA) was used for sensing lysozyme (Lys). HSA molecules were good stabilizing agents for AuNPs in high-salt solution and exhibited the ability to bond with Lys electrostatically. The aggregation of HSA-AuNPs was achieved upon the addition of high-pI proteins, such as Lys, alpha-chymotrypsinogen A, and conalbumin. Not the same was achieved, however, when low-pI proteins such as ovalbumin, bovine serum albumin, and alpha-lactalbumin were added. Matrix-assisted desorption/ionization mass spectrometry was used to demonstrate the interaction between HSA-AuNPs and Lys. It was found that the sensitivity of HSA-AuNPs for Lys was highly dependent on the HSA concentration. The Lys-induced aggregation of HSA-AuNPs was suggested based on the London-van der Waals attractive force. We further improved the selectivity of the probe by adjusting the pH solution to 8.0. Under the optimum conditions, the selectivity of this system for Lys over other proteins in high-salt solutions was remarkably high, even when their pI was very close to the Lys. The lowest detectable concentration of Lys in this approach was 50 nM. The applicability of the method was validated through the analyses of Lys in chicken egg white.
Chen
Yi-Ming
YM
Department of Chemistry, National Sun Yat-sen University, Taiwan.
Yu
Cheng-Ju
CJ
Cheng
Tian-Lu
TL
Tseng
Wei-Lung
WL
D000818:Animals; D002645:Chickens; D003124:Colorimetry / Q000379:methods*; D006046:Gold; D006801:Humans; D053768:Metal Nanoparticles; D009113:Muramidase / Q000032:analysis*; D055672:Static Electricity
D006046:Gold; D009113:Muramidase