Cargando…

Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking

The inhibition mechanism of two homoisoflavonoids from Ophiopogon japonicus including methylophiopogonanone A (MO-A) and methylophiopogonanone B (MO-B) on tyrosinase (Tyr) was studied by multiple spectroscopic techniques and molecular docking. The results showed that the two homoisoflavonoids both i...

Descripción completa

Detalles Bibliográficos
Autores principales: Wang, Liling, Qin, Yuchuan, Wang, Yanbin, Zhou, Yifeng, Liu, Bentong, Bai, Minge, Tong, Xiaoqing, Fang, Ru, Huang, Xubo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9042378/
https://www.ncbi.nlm.nih.gov/pubmed/35497266
http://dx.doi.org/10.1039/d1ra06091k
_version_ 1784694653058023424
author Wang, Liling
Qin, Yuchuan
Wang, Yanbin
Zhou, Yifeng
Liu, Bentong
Bai, Minge
Tong, Xiaoqing
Fang, Ru
Huang, Xubo
author_facet Wang, Liling
Qin, Yuchuan
Wang, Yanbin
Zhou, Yifeng
Liu, Bentong
Bai, Minge
Tong, Xiaoqing
Fang, Ru
Huang, Xubo
author_sort Wang, Liling
collection PubMed
description The inhibition mechanism of two homoisoflavonoids from Ophiopogon japonicus including methylophiopogonanone A (MO-A) and methylophiopogonanone B (MO-B) on tyrosinase (Tyr) was studied by multiple spectroscopic techniques and molecular docking. The results showed that the two homoisoflavonoids both inhibited Tyr activity via a reversible mixed-inhibition, with a half inhibitory concentration (IC(50)) of (10.87 ± 0.25) × 10(−5) and (18.76 ± 0.14) × 10(−5) mol L(−1), respectively. The fluorescence quenching and secondary structure change of Tyr caused by MO-A and B are mainly driven by hydrophobic interaction and hydrogen bonding. Molecular docking analysis indicated that phenylmalandioxin in MO-A and methoxy in MO-B could coordinate with a Cu ion in the active center of Tyr, and interacted with amino acid Glu322 to form hydrogen bonding, occupying the catalytic center to block the entry of the substrate and consequently inhibit Tyr activity. This study may provide new perspectives on the inhibition mechanism of MO-A and MO-B on Tyr and serve a scientific basis for screening effective Tyr inhibitors.
format Online
Article
Text
id pubmed-9042378
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher The Royal Society of Chemistry
record_format MEDLINE/PubMed
spelling pubmed-90423782022-04-28 Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking Wang, Liling Qin, Yuchuan Wang, Yanbin Zhou, Yifeng Liu, Bentong Bai, Minge Tong, Xiaoqing Fang, Ru Huang, Xubo RSC Adv Chemistry The inhibition mechanism of two homoisoflavonoids from Ophiopogon japonicus including methylophiopogonanone A (MO-A) and methylophiopogonanone B (MO-B) on tyrosinase (Tyr) was studied by multiple spectroscopic techniques and molecular docking. The results showed that the two homoisoflavonoids both inhibited Tyr activity via a reversible mixed-inhibition, with a half inhibitory concentration (IC(50)) of (10.87 ± 0.25) × 10(−5) and (18.76 ± 0.14) × 10(−5) mol L(−1), respectively. The fluorescence quenching and secondary structure change of Tyr caused by MO-A and B are mainly driven by hydrophobic interaction and hydrogen bonding. Molecular docking analysis indicated that phenylmalandioxin in MO-A and methoxy in MO-B could coordinate with a Cu ion in the active center of Tyr, and interacted with amino acid Glu322 to form hydrogen bonding, occupying the catalytic center to block the entry of the substrate and consequently inhibit Tyr activity. This study may provide new perspectives on the inhibition mechanism of MO-A and MO-B on Tyr and serve a scientific basis for screening effective Tyr inhibitors. The Royal Society of Chemistry 2021-10-22 /pmc/articles/PMC9042378/ /pubmed/35497266 http://dx.doi.org/10.1039/d1ra06091k Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Wang, Liling
Qin, Yuchuan
Wang, Yanbin
Zhou, Yifeng
Liu, Bentong
Bai, Minge
Tong, Xiaoqing
Fang, Ru
Huang, Xubo
Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking
title Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking
title_full Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking
title_fullStr Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking
title_full_unstemmed Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking
title_short Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking
title_sort inhibitory mechanism of two homoisoflavonoids from ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9042378/
https://www.ncbi.nlm.nih.gov/pubmed/35497266
http://dx.doi.org/10.1039/d1ra06091k
work_keys_str_mv AT wangliling inhibitorymechanismoftwohomoisoflavonoidsfromophiopogonjaponicusontyrosinaseactivityinsightfromspectroscopicanalysisandmoleculardocking
AT qinyuchuan inhibitorymechanismoftwohomoisoflavonoidsfromophiopogonjaponicusontyrosinaseactivityinsightfromspectroscopicanalysisandmoleculardocking
AT wangyanbin inhibitorymechanismoftwohomoisoflavonoidsfromophiopogonjaponicusontyrosinaseactivityinsightfromspectroscopicanalysisandmoleculardocking
AT zhouyifeng inhibitorymechanismoftwohomoisoflavonoidsfromophiopogonjaponicusontyrosinaseactivityinsightfromspectroscopicanalysisandmoleculardocking
AT liubentong inhibitorymechanismoftwohomoisoflavonoidsfromophiopogonjaponicusontyrosinaseactivityinsightfromspectroscopicanalysisandmoleculardocking
AT baiminge inhibitorymechanismoftwohomoisoflavonoidsfromophiopogonjaponicusontyrosinaseactivityinsightfromspectroscopicanalysisandmoleculardocking
AT tongxiaoqing inhibitorymechanismoftwohomoisoflavonoidsfromophiopogonjaponicusontyrosinaseactivityinsightfromspectroscopicanalysisandmoleculardocking
AT fangru inhibitorymechanismoftwohomoisoflavonoidsfromophiopogonjaponicusontyrosinaseactivityinsightfromspectroscopicanalysisandmoleculardocking
AT huangxubo inhibitorymechanismoftwohomoisoflavonoidsfromophiopogonjaponicusontyrosinaseactivityinsightfromspectroscopicanalysisandmoleculardocking