Next Article in Journal
Transient Co-Expression of Post-Transcriptional Gene Silencing Suppressors for Increased in Planta Expression of a Recombinant Anthrax Receptor Fusion Protein
Next Article in Special Issue
Fabrication, Modeling and Characterization of Multi-Crosslinked Methacrylate Copolymeric Nanoparticles for Oral Drug Delivery
Previous Article in Journal
Low Expression of TBX4 Predicts Poor Prognosis in Patients with Stage II Pancreatic Ductal Adenocarcinoma
Previous Article in Special Issue
Enhanced Anti-Tumoral Activity of Methotrexate-Human Serum Albumin Conjugated Nanoparticles by Targeting with Luteinizing Hormone-Releasing Hormone (LHRH) Peptide
Int. J. Mol. Sci. 2011, 12(8), 4964-4974; doi:10.3390/ijms12084964
Article

Interaction of Human Serum Album and C60 Aggregates in Solution

,
,
 and
*
Received: 30 March 2011 / Revised: 12 July 2011 / Accepted: 27 July 2011 / Published: 4 August 2011
(This article belongs to the Special Issue Bioactive Nanoparticles (special issue))
View Full-Text   |   Download PDF [533 KB, 19 June 2014; original version 19 June 2014]   |   Browse Figures

Abstract

An important property of C60 in aquatic ecotoxicology is that it can form stable aggregates with nanoscale dimensions, namely nC60. Aggregation allows fullerenes to remain suspended for a long time, and the reactivity of individual C60 is substantially altered in this aggregate form. Herein, we investigated the interaction of nC60 and human serum album (HSA) using the methods of fluorescence, fluorescence dynamics, circular dichroism (CD), and site marker competitive experiments. We proposed a binding model consistent with the available experimental results for the interactions of nC60 with HSA. During the interaction process, the structure and conformation of HSA were affected, leading to functional changes of drug binding sites of HSA.
Keywords: nC60; HSA; interaction; protein; fluorescence nC60; HSA; interaction; protein; fluorescence
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Share & Cite This Article

Further Mendeley | CiteULike
Export to BibTeX |
EndNote
MDPI and ACS Style

Song, M.; Liu, S.; Yin, J.; Wang, H. Interaction of Human Serum Album and C60 Aggregates in Solution. Int. J. Mol. Sci. 2011, 12, 4964-4974.

View more citation formats

Related Articles

Article Metrics

For more information on the journal, click here

Comments

Cited By

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert