Inhibitory Effects of Myriocin on Non-Enzymatic Glycation of Bovine Serum Albumin

Advanced glycation end products (AGEs) are the compounds produced by non-enzymatic glycation of proteins, which are involved in diabetic-related complications. To investigate the potential anti-glycation activity of Myriocin (Myr), a fungal metabolite of <i>Cordyceps</i>, the effect of M...

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Main Authors: Libo He, Yang Liu, Junling Xu, Jingjing Li, Guohua Cheng, Jiaxiu Cai, Jinye Dang, Meng Yu, Weiyan Wang, Wei Duan, Ke Liu
Format: Article
Language:English
Published: MDPI AG 2022-10-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/27/20/6995
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author Libo He
Yang Liu
Junling Xu
Jingjing Li
Guohua Cheng
Jiaxiu Cai
Jinye Dang
Meng Yu
Weiyan Wang
Wei Duan
Ke Liu
author_facet Libo He
Yang Liu
Junling Xu
Jingjing Li
Guohua Cheng
Jiaxiu Cai
Jinye Dang
Meng Yu
Weiyan Wang
Wei Duan
Ke Liu
author_sort Libo He
collection DOAJ
description Advanced glycation end products (AGEs) are the compounds produced by non-enzymatic glycation of proteins, which are involved in diabetic-related complications. To investigate the potential anti-glycation activity of Myriocin (Myr), a fungal metabolite of <i>Cordyceps</i>, the effect of Myr on the formation of AGEs resulted from the glycation of bovine serum albumin (BSA) and the interaction between Myr and BSA were studied by multiple spectroscopic techniques and computational simulations. We found that Myr inhibited the formation of AGEs at the end stage of glycation reaction and exhibited strong anti-fibrillation activity. Spectroscopic analysis revealed that Myr quenched the fluorescence of BSA in a static process, with the possible formation of a complex (approximate molar ratio of 1:1). The binding between BSA and Myr mainly depended on van der Waals interaction, hydrophobic interactions and hydrogen bond. The synchronous fluorescence and UV-visible (UV-<i>vis</i>) spectra results indicated that the conformation of BSA altered in the presence of Myr. The fluorescent probe displacement experiments and molecular docking suggested that Myr primarily bound to binding site 1 (subdomain IIA) of BSA. These findings demonstrate that Myr is a potential anti-glycation agent and provide a theoretical basis for the further functional research of Myr in the prevention and treatment of AGEs-related diseases.
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spelling doaj.art-a4ecab73099949d581396f719e9dad3f2023-11-24T01:35:20ZengMDPI AGMolecules1420-30492022-10-012720699510.3390/molecules27206995Inhibitory Effects of Myriocin on Non-Enzymatic Glycation of Bovine Serum AlbuminLibo He0Yang Liu1Junling Xu2Jingjing Li3Guohua Cheng4Jiaxiu Cai5Jinye Dang6Meng Yu7Weiyan Wang8Wei Duan9Ke Liu10Key Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, ChinaDepartment of Central Laboratory, The First People’s Hospital of Huzhou, First Affiliated Hospital of Huzhou University, Huzhou 313000, ChinaKey Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, ChinaKey Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, ChinaKey Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, ChinaKey Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, ChinaKey Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, ChinaKey Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, ChinaKey Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, ChinaSchool of Medicine, Deakin University, Geelong, VIC 3216, AustraliaKey Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, ChinaAdvanced glycation end products (AGEs) are the compounds produced by non-enzymatic glycation of proteins, which are involved in diabetic-related complications. To investigate the potential anti-glycation activity of Myriocin (Myr), a fungal metabolite of <i>Cordyceps</i>, the effect of Myr on the formation of AGEs resulted from the glycation of bovine serum albumin (BSA) and the interaction between Myr and BSA were studied by multiple spectroscopic techniques and computational simulations. We found that Myr inhibited the formation of AGEs at the end stage of glycation reaction and exhibited strong anti-fibrillation activity. Spectroscopic analysis revealed that Myr quenched the fluorescence of BSA in a static process, with the possible formation of a complex (approximate molar ratio of 1:1). The binding between BSA and Myr mainly depended on van der Waals interaction, hydrophobic interactions and hydrogen bond. The synchronous fluorescence and UV-visible (UV-<i>vis</i>) spectra results indicated that the conformation of BSA altered in the presence of Myr. The fluorescent probe displacement experiments and molecular docking suggested that Myr primarily bound to binding site 1 (subdomain IIA) of BSA. These findings demonstrate that Myr is a potential anti-glycation agent and provide a theoretical basis for the further functional research of Myr in the prevention and treatment of AGEs-related diseases.https://www.mdpi.com/1420-3049/27/20/6995Myriocinnon-enzymatic glycationBSAspectroscopic techniquescomputational simulations
spellingShingle Libo He
Yang Liu
Junling Xu
Jingjing Li
Guohua Cheng
Jiaxiu Cai
Jinye Dang
Meng Yu
Weiyan Wang
Wei Duan
Ke Liu
Inhibitory Effects of Myriocin on Non-Enzymatic Glycation of Bovine Serum Albumin
Molecules
Myriocin
non-enzymatic glycation
BSA
spectroscopic techniques
computational simulations
title Inhibitory Effects of Myriocin on Non-Enzymatic Glycation of Bovine Serum Albumin
title_full Inhibitory Effects of Myriocin on Non-Enzymatic Glycation of Bovine Serum Albumin
title_fullStr Inhibitory Effects of Myriocin on Non-Enzymatic Glycation of Bovine Serum Albumin
title_full_unstemmed Inhibitory Effects of Myriocin on Non-Enzymatic Glycation of Bovine Serum Albumin
title_short Inhibitory Effects of Myriocin on Non-Enzymatic Glycation of Bovine Serum Albumin
title_sort inhibitory effects of myriocin on non enzymatic glycation of bovine serum albumin
topic Myriocin
non-enzymatic glycation
BSA
spectroscopic techniques
computational simulations
url https://www.mdpi.com/1420-3049/27/20/6995
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