Home
Resources
Publications
Inhibitory Potential of Polyhdroxylated Fullerenes against Protein Tyrosine Phosphatase 1B

Inhibitory Potential of Polyhdroxylated Fullerenes against Protein Tyrosine Phosphatase 1B

O L Kobzar, V V Trush, V Yu Tanchuk, A I Vovk

Ukr Biochem J. Jul-Aug 2015;87(4):24-31.

PMID: 26547960

Abstract:

Inhibition of PTP1B by polyhydroxylated fullerenes was studied in silico and in vitro. The enzyme kinetics in the presence of polyhydroxy small gap fullerenes showed that reciprocal value of maximum velocity non-linearly increases with increasing the inhibitor concentration. Analysis of the dose-dependent curve of PTP1B inhibition suggests an apparent positive cooperativity with involvement of at least two binding sites for the hydroxylated fullerene cages. Molecular docking calculations indicated that highly hydroxylated fullerene C60 may occupy the active site and additional allosteric binding site with similar affinity. In silico analysis of a number of fullerenols with 6, 12, 18, 24, 30, and 36 hydroxyl groups showed that the inhibitory activity may depend on the degree of hydroxylation of the nanoparticles surface. These data provide some understanding of the mechanisms of inhibitory action of fullerenols on activity of protein tyrosine phosphatases.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
LS721017	Small gap fullerenes			Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: