Effect of particle size on conformation and enzymatic activity of EcoRI adsorbed on CdS nanoparticles

Colloids Surf B Biointerfaces. 2014 Feb 1:114:269-76. doi: 10.1016/j.colsurfb.2013.10.020. Epub 2013 Oct 22.

Abstract

Better understanding of the interaction between nanoparticles (NPs) and protein is the basis for biological and biomedical applications of NPs. Water-soluble fluorescent CdS NPs have been widely used in the biological and biomedical fields and the study on effect of CdS NPs size on conformation and enzymatic activity of protein might be very important in its application. In this work, the interaction of CdS NPs with different size with type II restriction endonuclease (EcoRI) were investigated by atomic force microscopy, transmission electron microscopy, UV-vis spectroscopy, fluorescence quenching method, CD spectra, laser scanning confocal microscopy and gel electrophoresis. It was found that the equilibrium constant (kD) as well as the cooperativity degree of CdS NPs-EcoRI binding (Hill constant, n) strongly depended on the CdS NPs size. The different curvature of CdS NPs surface could result in different changes of EcoRI conformation. The gel electrophoresis indicated that the decrease in α-helix content more or less affected the activity of EcoRI.

Keywords: CdS nanoparticles; Conformation change; Cooperativity; EcoRI; Enzymatic activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Cadmium Compounds / chemistry*
  • Circular Dichroism
  • Deoxyribonuclease EcoRI / chemistry*
  • Deoxyribonuclease EcoRI / metabolism*
  • Enzyme Assays
  • Microscopy, Atomic Force
  • Nanoparticles / chemistry*
  • Nanoparticles / ultrastructure
  • Particle Size*
  • Protein Conformation
  • Spectrometry, Fluorescence
  • Spectrophotometry, Ultraviolet
  • Sulfides / chemistry*

Substances

  • Cadmium Compounds
  • Sulfides
  • cadmium sulfide
  • Deoxyribonuclease EcoRI