Molecular interaction study of flavonoids with human serum albumin using native mass spectrometry and molecular modeling

doi:10.1007/s00216-017-0564-7

	Molecular interaction study of flavonoids with human serum albumin using native mass spectrometry and molecular modeling
	Wang, Bohong 1,2; Qin, Qian 1,2; Chang, Mengmeng 1,2; Li, Shuyan 3; Shi, Xianzhe 2; Xu, Guowang 2
刊名	ANALYTICAL AND BIOANALYTICAL CHEMISTRY
	2018
卷号	410 期号:3 页码:827-837
关键词	Native Mass Spectrometry Noncovalent Interaction Human Serum Albumin Flavonoids
ISSN号	1618-2642
DOI	10.1007/s00216-017-0564-7
文献子类	Article
英文摘要	Noncovalent interactions between proteins and small-molecule ligands widely exist in biological bodies and play significant roles in many physiological and pathological processes. Native mass spectrometry (MS) has emerged as a new powerful tool to study noncovalent interactions by directly analyzing the ligand-protein complexes. In this work, an ultrahigh-resolution native MS method based on a 15-T SolariX XR Fourier transform ion cyclotron resonance mass spectrometer was firstly used to investigate the interaction between human serum albumin (HSA) and flavonoids. Various flavonoids with similar structure were selected to unravel the relationship between the structure of flavonoids and their binding affinity for HSA. It was found that the position of the hydroxyl groups and double bond of flavonoids could influence the noncovalent interaction. Through a competitive experiment between HSA binding site markers and apigenin, the subdomain IIA (site 1) of HSA was determined as the binding site for flavonoids. Moreover, a cooperative allosteric interaction between apigenin and ibuprofen was found from their different HSA binding sites, which was further verified by circular dichroism spectroscopy and molecular docking studies. These results show that native MS is a useful tool to investigate the molecular interaction between a protein and its ligands.
WOS关键词	FLUORESCENCE SPECTROSCOPY ; NONCOVALENT INTERACTIONS ; CYTOCHROME-C ; ESI-MS ; BINDING ; DOCKING ; SIMULATIONS ; RESOLUTION ; CONSTANTS ; PROTEINS
WOS研究方向	Biochemistry & Molecular Biology ; Chemistry
语种	英语
出版者	SPRINGER HEIDELBERG
WOS记录号	WOS:000422952600013
内容类型	期刊论文
源URL	[http://cas-ir.dicp.ac.cn/handle/321008/168538]
专题	大连化学物理研究所_中国科学院大连化学物理研究所
通讯作者	Shi, Xianzhe; Xu, Guowang
作者单位	1.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 2.Chinese Acad Sci, Dalian Inst Chem Phys, CAS Key Lab Separat Sci Analyt Chem, Dalian 116023, Liaoning, Peoples R China 3.Lanzhou Univ, Coll Chem & Chem Engn, Lanzhou 730000, Gansu, Peoples R China
推荐引用方式 GB/T 7714	Wang, Bohong,Qin, Qian,Chang, Mengmeng,et al. Molecular interaction study of flavonoids with human serum albumin using native mass spectrometry and molecular modeling[J]. ANALYTICAL AND BIOANALYTICAL CHEMISTRY,2018,410(3):827-837.
APA	Wang, Bohong,Qin, Qian,Chang, Mengmeng,Li, Shuyan,Shi, Xianzhe,&Xu, Guowang.(2018).Molecular interaction study of flavonoids with human serum albumin using native mass spectrometry and molecular modeling.ANALYTICAL AND BIOANALYTICAL CHEMISTRY,410(3),827-837.
MLA	Wang, Bohong,et al."Molecular interaction study of flavonoids with human serum albumin using native mass spectrometry and molecular modeling".ANALYTICAL AND BIOANALYTICAL CHEMISTRY 410.3(2018):827-837.