TY - JOUR
T1 - Pannorin isolated from marine Penicillium sp. SG-W3
T2 - a selective monoamine oxidase A inhibitor
AU - Oh, Jong Min
AU - Gao, Qian
AU - Shin, Woong Hee
AU - Lee, Eun Young
AU - Chung, Dawoon
AU - Choi, Grace
AU - Nam, Sang Jip
AU - Kim, Hoon
N1 - Publisher Copyright:
© The Author(s) 2024.
PY - 2024/12
Y1 - 2024/12
N2 - Six compounds were isolated from Penicillium sp. SG-W3, a marine-derived fungus, and their inhibitory activities against target enzymes relating to neurological diseases were evaluated. Compound 1 (pannorin) was a potent and selective monoamine oxidase (MAO)-A inhibitor with a 50% inhibitory concentration (IC50) of 1.734 μM and a selectivity index (SI) of > 23.07 versus MAO-B, and it showed an efficient antioxidant activity. All compounds showed weak inhibitory activities against acetylcholinesterase, butyrylcholinesterase, and β-secretase. The inhibition constant (Ki) of 1 for MAO-A was 1.049 ± 0.030 μM with competitive inhibition. Molecular docking simulation predicted that compound 1 forms hydrogen bonds with MAO-A, and binds more tightly to MAO-A than to MAO-B (− 25.02 and − 24.06 kcal/mol, respectively). These results suggest that compound 1 is a selective, reversible, and competitive MAO-A inhibitor that can be a therapeutic candidate for treating neurological diseases.
AB - Six compounds were isolated from Penicillium sp. SG-W3, a marine-derived fungus, and their inhibitory activities against target enzymes relating to neurological diseases were evaluated. Compound 1 (pannorin) was a potent and selective monoamine oxidase (MAO)-A inhibitor with a 50% inhibitory concentration (IC50) of 1.734 μM and a selectivity index (SI) of > 23.07 versus MAO-B, and it showed an efficient antioxidant activity. All compounds showed weak inhibitory activities against acetylcholinesterase, butyrylcholinesterase, and β-secretase. The inhibition constant (Ki) of 1 for MAO-A was 1.049 ± 0.030 μM with competitive inhibition. Molecular docking simulation predicted that compound 1 forms hydrogen bonds with MAO-A, and binds more tightly to MAO-A than to MAO-B (− 25.02 and − 24.06 kcal/mol, respectively). These results suggest that compound 1 is a selective, reversible, and competitive MAO-A inhibitor that can be a therapeutic candidate for treating neurological diseases.
KW - Enzyme kinetics
KW - Molecular docking and dynamics
KW - Monoamine oxidase
KW - Pannorin
KW - Penicillium sp. SG-W3
KW - Reversible competitive inhibitor
UR - http://www.scopus.com/inward/record.url?scp=85186562699&partnerID=8YFLogxK
U2 - 10.1186/s13765-024-00878-7
DO - 10.1186/s13765-024-00878-7
M3 - Article
AN - SCOPUS:85186562699
SN - 2468-0834
VL - 67
JO - Applied Biological Chemistry
JF - Applied Biological Chemistry
IS - 1
M1 - 26
ER -
