The in vitro inhibition effect of 2 nm gold nanoparticles on non-enzymatic glycation of human serum albumin

Biochem Biophys Res Commun. 2012 Jun 8;422(3):447-54. doi: 10.1016/j.bbrc.2012.05.014. Epub 2012 May 10.

Abstract

The reaction of amino groups of protein and the carbonyl groups of reducing sugar molecules, non-enzymatically induce a series of chemical reactions that form a heterogeneous group of compounds known as advanced glycation end products (AGEs). The accumulation of AGEs is associated with various disease conditions that include complications in diabetes, Alzheimer's disease and aging. The current study monitored the extent of non-enzymatic glycation of human serum albumin (HSA) in order to estimate the formation of HSA related AGEs in the presence of 2 nm gold nanoparticles. The rate of glycation was evaluated using several analytical methods. Physiological concentrations of HSA and glyceraldehyde mixtures, incubated with various concentrations of negatively charged 2 nm gold nanoparticles, resulted in a lower reaction rate than mixtures without 2GNP. Moreover, increasing concentrations of gold nanoparticles exhibited a pronounced reduction in AGE formation. High performance liquid chromatography, UV-visible spectroscopy and circular dichroism analytical methods provide reliable techniques for evaluating AGE formation of HSA adducts.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, High Pressure Liquid
  • Glycation End Products, Advanced / analysis
  • Glycation End Products, Advanced / antagonists & inhibitors*
  • Glycosylation / drug effects
  • Gold / chemistry
  • Gold / pharmacology*
  • Humans
  • Metal Nanoparticles / chemistry*
  • Protein Structure, Secondary
  • Serum Albumin / chemistry*

Substances

  • Glycation End Products, Advanced
  • Serum Albumin
  • Gold