NDLI: The Interaction of Flavonoid-Lysozyme and the Relationship Between Molecular Structure of Flavonoids and Their Binding Activity to Lysozyme

Content Provider	Springer Nature Link
Author	Yang, Ran Yu, Lanlan Zeng, Huajin Liang, Ruiling Chen, Xiaolan Qu, Lingbo
Copyright Year	2012
Abstract	In this work, the interactions of twelve structurally different flavonoids with Lysozyme (Lys) were studied by fluorescence quenching method. The interaction mechanism and binding properties were investigated. It was found that the binding capacities of flavonoids to Lys were highly depend on the number and position of hydrogen, the kind and position of glycosyl. To explore the selectivity of the bindings of flavonoids with Lys, the structure descriptors of the flavonoids were calculated under QSAR software package of Cerius2, the quantitative relationship between the structures of flavonoids and their binding activities to Lys (QSAR) was performed through genetic function approximation (GFA) regression analysis. The QSAR regression equation was K $_{A}$ = 37850.460 + 1630.01Dipole +3038.330HD-171.795MR. (r = 0.858, $$ r_{\text{CV}}^2 = 0.444 $$ , F $_{(11,3)}$ = 7.48), where K $_{A}$ is binding constants, Dipole, HD and MR was dipole moment, number of hydrogen-bond donor and molecular refractivity, respectively. The obtained results make us understand better how the molecular structures influencing their binding to protein which may open up new avenues for the design of the most suitable flavonoids derivatives with structure variants.
Starting Page	1449
Ending Page	1459
Page Count	11
File Format	PDF
ISSN	10530509
Journal	Journal of Fluorescence
Volume Number	22
Issue Number	6
e-ISSN	15734994
Language	English
Publisher	Springer US
Publisher Date	2012-07-08
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Flavonoids Fluorescence quenching Molecular modeling techniques Quantitative structure-activity relationship (QSAR) Biophysics and Biological Physics Biomedicine general Analytical Chemistry Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Sociology and Political Science Spectroscopy Law Biochemistry Clinical Biochemistry Clinical Psychology

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1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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