Skip to main content

Effect of Cadmium Sulfide Quantum Dots on Physical Properties of R-Phycoerythrin as a Protein Matrix

Buy Article:

$63.00 plus tax (Refund Policy)

The synthesis and analysis of nanostructures in the cavities of protein molecules is a promising research field in the industry of nanosystems. In this study, atomic force microscopy (AFM) has been used to evaluate the properties of CdS quantum dots synthesized in the tunnel cavities of R-phycoerythrin, a 290 kDa water-soluble pigment protein responsible for light harvesting in red algae. It has been shown that R-phycoerythrin dissolved in deionized water to a concentration of 50 μg/ml is prone to self-organization into regular spatial structures upon adsorption on the surface of mica, but no such structuring takes place in films prepared from R-phycoerythrin solutions diluted tenfold. In the latter case, protein molecules are deformed, as judged from the analysis of the surface profile. R-phycoerythrin with CdS quantum dots in protein cavities (the concentration of the preparation was (48 μg/ml) loses the self-organization ability and is not deformed upon adsorption on the mica surface. Analysis of AFM images by flicker-noise spectroscopy has shown that incorporation of CdS quantum dots into R-phycoerythrin molecules provides for “smoothing” of the protein surface, with various irregularities being leveled off. Conversely, the irregularity of the protein surface increases when R-phycoerythrin molecules are arranged into three-dimensional branching structures. It is concluded that CdS quantum dots interfere with protein–protein interactions and restrain the conformational mobility of the protein. The anomalously rigid structure of Rphycoerythrin in the presence of CdS is due to its conformational rearrangements during the synthesis of quantum dot.
No References
No Citations
No Supplementary Data
No Data/Media
No Metrics

Keywords: CdS nanoparticles; Quantum dots; R-phycoerythrin; atomic force microscopy; biomacromolecules; conformational mobility; flicker-noise spectroscopy; nanostructures; protein molecules; protein–protein interactions

Document Type: Research Article

Publication date: 2013-01-01

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more