Open AccessInteraction between PET tracer and the specific residues around the gate of the open form of Monoamine Oxidase B (MAO-B)
Author(s) -
M Ottawa,
Naoyuki Miyashita
Publication year - 2022
Publication title -
journal of physics. conference series
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.21
H-Index - 85
eISSN - 1742-6596
pISSN - 1742-6588
DOI - 10.1088/1742-6596/2207/1/012025
Subject(s) - monoamine oxidase a , monoamine oxidase , monoamine oxidase b , chemistry , monoamine neurotransmitter , binding site , docking (animal) , stereochemistry , enzyme , biophysics , biochemistry , biology , receptor , medicine , serotonin , nursing
Monoamine Oxidase B (MAO-B) is the enzyme that metabolizes a monoamine neurotransmitter. Recently, a PET tracer targeting MAO-B, SMBT-1, has been developed as the biomarker of neurodegenerative diseases. However, the detailed binding mode of SMBT-1 has not been clear. To clarify the binding mode of SMBT-1 on MAO-B, we performed the molecular dynamics (MD) simulations of MAO-B in the outer mitochondrial membrane and the complex of MAO-B to SMBT-1, and the docking simulation of MAO-B with SMBT-1. We found that the Leu 88 , Leu 171 , Ile 199 , and Tyr 326 around the substrate-binding site interact with SMBT-1. These hydrophobic residues mainly support the two aromatic rings of the center of SMBT-1, making the stable binding of SMBT-1.