Interaction of Human Serum Album and C60 Aggregates in Solution

Maoyong Song,Shufang Liu,Junfa Yin,Hailin Wang

doi:10.3390/ijms12084964

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.

Highlights

Since the discovery of fullerene (C60) in 1985 [1], concerns have been raised about the proposed applications of C60 and its derivatives in biology and pharmacology [2,3]
Our results above indicate that the fluorescence quenching and conformational changes of human serum albumin (HSA) can be attributed to the interaction between HSA and nC60
We observed a quenching of fluorescence of HSA in the presence of nC60, and fluorescence quenching mechanism was investigated by the Stern-Volmer equation which showed a characteristic feature for the combined fluorescence quenching

Summary

Introduction

Since the discovery of fullerene (C60) in 1985 [1], concerns have been raised about the proposed applications of C60 and its derivatives in biology and pharmacology [2,3]. These potential applications include items as varied as antiviral, anticancer, or antioxidant agents [4], and drug delivery vehicles [5,6]. For C60 fullerene, its interaction with proteins has been poorly studied due in particular to its low solubility in water, and much research has focused on the interactions between its water-soluble derivatives and some proteins such as HIV protease [9,10], a fullerene-specific antibody [11], human serum albumin (HSA) [12] and bovine serum albumin (BSA) [13]

Methods

Results

Conclusion