PMID- 25669664
OWN - NLM
STAT- MEDLINE
DCOM- 20160819
LR  - 20161125
IS  - 1522-7243 (Electronic)
IS  - 1522-7235 (Linking)
VI  - 30
IP  - 7
DP  - 2015 Nov
TI  - Resonance energy transfer, pH-induced folded states and the molecular interaction 
      of human serum albumin and icariin.
PG  - 1026-33
LID - 10.1002/bio.2854 [doi]
AB  - Icariin is a flavonol glycoside with a wide range of pharmacological and 
      biological activities. The pharmacological and biological functions of flavonoid 
      compounds mainly originate from their binding to proteins. The mode of 
      interaction of icariin with human serum albumin (HSA) has been characterized by 
      fluorescence spectroscopy and far- and near-UV circular dichroism (CD) 
      spectroscopy under different pH conditions. Fluorescence quenching studies showed 
      that the binding affinity of icariin with HSA in the buffer solution at different 
      pH values is: Ka (pH 4.5) > Ka (pH 3.5) > Ka (pH 9.0) > Ka (pH 7.0). Red-edge 
      excitation shift (REES) studies revealed that pH had an obvious effect on the 
      mobility of the tryptophan microenvironment and the addition of icariin made the 
      REES effect more distinct. The static quenching mechanism and number of binding 
      sites (n  approximately  1) were obtained from fluorescence data at three temperatures (298, 
      304 and 310 K). Both ∆H(0) < 0 and ∆capital DSE, Macedonian(0) < 0 suggested that hydrogen bonding and 
      van der Waal's interaction were major driving forces in the binding mechanism, 
      and this was also confirmed by the molecular simulation results. The distance r 
      between the donor (HSA) and the acceptor (icariin) was calculated based on 
      Forster non-radiation energy transfer theory. We found that pH had little impact 
      on the energy transfer between HSA and icariin. Far- and near-UV CD spectroscopy 
      studies further indicated the influence of pH on the complexation process and the 
      alteration in the protein conformation upon binding.
CI  - Copyright (c) 2015 John Wiley & Sons, Ltd.
FAU - Cheng, Xiao-Xia
AU  - Cheng XX
AD  - State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for 
      Biology and Medicine (MOE), College of Chemistry and Molecular Sciences, Wuhan 
      University, Wuhan, 430072, People's Republic of China.
AD  - School of Chemistry, Chemical Engineering and Life Sciences, Wuhan University of 
      Technology, Wuhan, 430072, People's Republic of China.
FAU - Fan, Xiao-Yang
AU  - Fan XY
AD  - State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for 
      Biology and Medicine (MOE), College of Chemistry and Molecular Sciences, Wuhan 
      University, Wuhan, 430072, People's Republic of China.
FAU - Jiang, Feng-Lei
AU  - Jiang FL
AD  - State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for 
      Biology and Medicine (MOE), College of Chemistry and Molecular Sciences, Wuhan 
      University, Wuhan, 430072, People's Republic of China.
FAU - Liu, Yi
AU  - Liu Y
AD  - State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for 
      Biology and Medicine (MOE), College of Chemistry and Molecular Sciences, Wuhan 
      University, Wuhan, 430072, People's Republic of China.
FAU - Lei, Ke-Lin
AU  - Lei KL
AD  - School of Chemistry and Food Sciences, Hubei University of Arts and Sciences, 
      Xiangyang, 441053, People's Republic of China.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20150209
PL  - England
TA  - Luminescence
JT  - Luminescence : the journal of biological and chemical luminescence
JID - 100889025
RN  - 0 (Flavonoids)
RN  - 0 (Serum Albumin)
RN  - VNM47R2QSQ (icariin)
SB  - IM
MH  - Circular Dichroism
MH  - Energy Transfer
MH  - Flavonoids/*chemistry
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Molecular Docking Simulation
MH  - Protein Folding
MH  - Serum Albumin/*chemistry
MH  - Spectrometry, Fluorescence
MH  - Temperature
OTO - NOTNLM
OT  - circular dichroism spectroscopy
OT  - energy transfer
OT  - fluorescence spectroscopy
OT  - icariin
OT  - pH
EDAT- 2015/02/12 06:00
MHDA- 2016/08/20 06:00
CRDT- 2015/02/12 06:00
PHST- 2014/07/19 00:00 [received]
PHST- 2014/12/15 00:00 [revised]
PHST- 2014/12/28 00:00 [accepted]
PHST- 2015/02/12 06:00 [entrez]
PHST- 2015/02/12 06:00 [pubmed]
PHST- 2016/08/20 06:00 [medline]
AID - 10.1002/bio.2854 [doi]
PST - ppublish
SO  - Luminescence. 2015 Nov;30(7):1026-33. doi: 10.1002/bio.2854. Epub 2015 Feb 9.