CdTe quantum dots (QDs) improve the affinities of baicalein and genistein for human serum albumin in vitro

J Inorg Biochem. 2010 Nov;104(11):1148-55. doi: 10.1016/j.jinorgbio.2010.07.003. Epub 2010 Jul 17.

Abstract

Baicalein and genistein were studied for the affinities for human serum albumin (HSA) in the presence and absence of three CdTe quantum dots (QDs) with different sizes. Three typical CdTe QDs with maximum emissions of 535 nm (green-emitting, G-QDs), 598 nm (yellow-emitting, Y-QDs), and 654 nm (red-emitting, R-QDs) were tested. The fluorescence intensities of HSA decreased remarkably with increasing concentration of QDs. Baicalein resulted in an obvious blue-shift of the λ(em) of HSA from 340 to 334 nm. However, the extents of blue-shifts induced by baicalein and genistein in the presence of QDs were much bigger than that in the absence of QDs. The quenching process of baicalein for HSA was easily affected by the QDs size than that of genistein. QDs increased the quenching constant from 136.97% to 162.24% for baicalein. However, QDs only increased the quenching constants from 20.56% to 32.23% for genistein. G-QDs, Y-QDs, and R-QDs increased the affinities of baicalein for HSA about 3.02%, 6.38% and 9.40%. G-QDs, Y-QDs, and R-QDs increased the affinities of genistein for HSA about 2.56%, 13.46% and 19.44%. The binding affinities of baicalein and genistein for HSA increased with increasing QDs size.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Albumins / metabolism*
  • Cadmium / chemistry*
  • Flavanones / chemistry
  • Flavanones / metabolism*
  • Genistein / chemistry
  • Genistein / metabolism*
  • Humans
  • Molecular Structure
  • Quantum Dots*
  • Serum Albumin / chemistry*
  • Spectrometry, Fluorescence / methods
  • Tellurium / chemistry*

Substances

  • Albumins
  • Flavanones
  • Serum Albumin
  • Cadmium
  • baicalein
  • Genistein
  • Tellurium