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Molecules 2017, 22(7), 1036; doi:10.3390/molecules22071036

Molecular Structure–Affinity Relationship of Flavonoids in Lotus Leaf (Nelumbo nucifera Gaertn.) on Binding to Human Serum Albumin and Bovine Serum Albumin by Spectroscopic Method

1
Hubei Key Laboratory of Edible Wild Plants Conservation and Utilization & National Demonstration Center for Experimental Biology Education & College of Life Sciences, Hubei Key Laboratory of Pollutant Analysis & Reuse Technology, Hubei Normal University, Huangshi 435002, China
2
Institute of Bast Fiber Crops, Chinese Academy of Agricultural Sciences, Changsha 410205, China
3
School of Environmental Science and Engineering, Hubei Polytechnic University, Hubei Key Laboratory of Mine Environmental Pollution Control and Remediation, Huangshi 435003, China
*
Author to whom correspondence should be addressed.
Received: 3 May 2017 / Revised: 20 June 2017 / Accepted: 20 June 2017 / Published: 23 June 2017
(This article belongs to the Section Natural Products)
View Full-Text   |   Download PDF [1471 KB, uploaded 23 June 2017]   |  

Abstract

Lotus leaf has gained growing popularity as an ingredient in herbal formulations due to its various activities. As main functional components of lotus leaf, the difference in structure of flavonoids affected their binding properties and activities. In this paper, the existence of 11 flavonoids in lotus leaf extract was confirmed by High Performance Liquid Chromatography (HPLC) analysis and 11 flavonoids showed various contents in lotus leaf. The interactions between lotus leaf extract and two kinds of serum albumins (human serum albumin (HSA) and bovine serum albumin (BSA)) were investigated by spectroscopic methods. Based on the fluorescence quenching, the interactions between these flavonoids and serum albumins were further checked in detail. The relationship between the molecular properties of flavonoids and their affinities for serum albumins were analyzed and compared. The hydroxylation on 3 and 3’ position increased the affinities for serum albumins. Moreover, both of the methylation on 3’ position of quercetin and the C2=C3 double bond of apigenin and quercetin decreased the affinities for HSA and BSA. The glycosylation lowered the affinities for HSA and BSA depending on the type of sugar moiety. It revealed that the hydrogen bond force played an important role in binding flavonoids to HSA and BSA. View Full-Text
Keywords: bovine serum albumin; flavonoids; fluorescence spectroscopy; human serum albumin; interaction; lotus leaf bovine serum albumin; flavonoids; fluorescence spectroscopy; human serum albumin; interaction; lotus leaf
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Tang, X.; Tang, P.; Liu, L. Molecular Structure–Affinity Relationship of Flavonoids in Lotus Leaf (Nelumbo nucifera Gaertn.) on Binding to Human Serum Albumin and Bovine Serum Albumin by Spectroscopic Method. Molecules 2017, 22, 1036.

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