Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques.

Shufang Liu,Zhanzuo Liu,Shu’E Wang

doi:10.3390/ma14020298

Abstract

The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.

Highlights

As a kind of classic carbon nanomaterial, due to their unique structural characteristics and physical and chemical properties, nC60 nanomaterials and their derivatives have great application potential in many fields, such as chemistry, life sciences, materials sciences, and biomedicine. [1,2,3]
We found that particle size has an obvious effect on the binding of nC60 to human serum albumin (HSA) and bovine serum albumin (BSA). nC60 nanoparticles with smaller size distribution have stronger binding to HSA/BSA proteins
We used the fluorescence method to study the fluorescence of proteins (BSA and HSA) with a dose–response relationship, and the the interaction nC

Summary

Introduction

As a kind of classic carbon nanomaterial, due to their unique structural characteristics and physical and chemical properties, nC60 nanomaterials and their derivatives have great application potential in many fields, such as chemistry, life sciences, materials sciences, and biomedicine. [1,2,3]. As a kind of classic carbon nanomaterial, due to their unique structural characteristics and physical and chemical properties, nC60 nanomaterials and their derivatives have great application potential in many fields, such as chemistry, life sciences, materials sciences, and biomedicine. Due to the limitation of experimental methods, the types and quantity of modification groups of nC60 derivatives obtained by different research groups are different, which leads to the lack of comparability of data among different research groups. Even for the study of the interaction between pristine nC60 and proteins, due to the different preparation methods of nC60 nanoparticles, the morphology characteristics (morphology, size, particle size distribution, surface area, etc.) of nC60 aqueous dispersion obtained by different research groups are different, so the research results of different research groups are not completely consistent

Objectives

Methods

Results

Conclusion