Background: Nilatinib is an irreversible tyrosine kinase inhibitor, which is used in the
treatment of some kinds of cancer. To study the interaction between Neratinib and MAD2L1, a potential
tumor target, is of guiding significance for enriching the medicinal value of Neratinib.
Method: The binding mechanism between Mitotic arrest deficient 2-like protein 1 (MAD2L1) and
Neratinib under simulative physiological conditions was investigated by molecule simulation and
Results: Molecular docking showed the most possible binding mode of Neratinib-MAD2L1 and the
potential binding sites and interaction forces of the interaction between MAD2L1 and Neratinib.
Fluorescence spectroscopy experiments manifested that Neratinib could interact with MAD2L1 and
form a complex by hydrogen bond and van der Waals interaction. These results were consistent with
the conclusions obtained from molecular docking. In addition, according to Synchronous fluorescence
and three-dimensional fluorescence results, Neratinib might lead to the conformational change
of MAD2L1, which may affect the biological functions of MAD2L1.
Conclusion: This study indicated that Neratinib could interact with MAD2L1 and lead to the conformational
change of MAD2L1. These works provide helpful insights for the further study of biological
function of MAD2L1 and novel pharmacological utility of Neratinib.