https://orcid.org/0000-0002-0165-4108
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Abstract
In the present work, we studied the inhibitory and kinetic implications of classical PTP1B inhibitors (chlorogenic acid, ursolic acid, suramin) using three enzyme constructs (hPTP1B1-285, hPTP1B1-321, and hPTP1B1-400). The results indicate that the unstructured region of PTP1B (300-400 amino acids) is very important both to obtain optimal inhibitory results and propose classical inhibition mechanisms (competitive or non-competitive) through kinetic studies. The IC50 calculated for ursolic acid and suramin using hPTP1B1-400 are around four and three times lower to the short form of the enzyme, the complete form of PTP1B, the one found in the cytosol (in vivo). On the other hand, we highlight the studies of enzymatic kinetics using the hPTP1B1-400 to know the type of enzymatic inhibition and to be able to direct docking studies, where the unstructured region of the enzyme can be one more option for binding compounds with inhibitory activity.
GRAPHICAL ABSTRACT
Acknowledgements
The authors are very grateful to the Research Division of the Medical School, UNAM. We are indebted to Dirección General de Cómputo y de Tecnologías de Información y Comunicación, UNAM, for providing the resources to carry out computational calculations through Miztli System. The authors acknowledge the invaluable technical support of María del Rocío Álvaresz Medina, María Isabel Velázquez López, Eugenia Flores Robles, and Laura Iliana Alvarez Añorve.
Disclosure statement
No potential conflict of interest was reported by the autor(s).