PMID- 24802274
OWN - NLM
STAT- MEDLINE
DCOM- 20140729
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1838
IP  - 8
DP  - 2014 Aug
TI  - Lipid binding specificity of bovine alpha-lactalbumin: a multidimensional approach.
PG  - 2078-86
LID - S0005-2736(14)00162-X [pii]
LID - 10.1016/j.bbamem.2014.04.027 [doi]
AB  - Many soluble proteins are known to interact with membranes in partially 
      disordered states, and the mechanism and relevance of such interactions in 
      cellular processes are beginning to be understood. Bovine alpha-lactalbumin (BLA) 
      represents an excellent prototype for monitoring membrane interaction due to its 
      conformational plasticity. In this work, we comprehensively monitored the 
      interaction of apo-BLA with zwitterionic and negatively charged membranes 
      utilizing a variety of approaches. We show that BLA preferentially binds to 
      negatively charged membranes at acidic pH with higher binding affinity. This is 
      supported by spectral changes observed with a potential-sensitive membrane probe 
      and fluorescence anisotropy measurements of a hydrophobic probe. Our results show 
      that BLA exhibits a molten globule conformation when bound to negatively charged 
      membranes. We further show, using the parallax approach, that BLA penetrates the 
      interior of negatively charged membranes, and tryptophan residues are localized 
      at the membrane interface. Red edge excitation shift (REES) measurements reveal 
      that the immediate environment of tryptophans in membrane-bound BLA is 
      restricted, and the restriction is dependent on membrane lipid composition. We 
      envision that understanding the mechanism of BLA-membrane interaction would help 
      in bioengineering of alpha-lactalbumin, and to address the mechanism of tumoricidal 
      and antimicrobial activities of BLA-oleic acid complex.
CI  - Copyright (c) 2014 Elsevier B.V. All rights reserved.
FAU - Chaudhuri, Arunima
AU  - Chaudhuri A
AD  - CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, 
      India.
FAU - Chattopadhyay, Amitabha
AU  - Chattopadhyay A
AD  - CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, 
      India. Electronic address: amit@ccmb.res.in.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140504
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Apoproteins)
RN  - 0 (Lipid Bilayers)
RN  - 0 (apo-alpha-lactalbumin)
RN  - 2UMI9U37CP (Oleic Acid)
RN  - 8DUH1N11BX (Tryptophan)
RN  - 9013-90-5 (Lactalbumin)
SB  - IM
MH  - Animals
MH  - Apoproteins/chemistry/*metabolism
MH  - Cattle
MH  - Circular Dichroism
MH  - Fluorescence Polarization
MH  - Lactalbumin/chemistry/*metabolism
MH  - Lipid Bilayers/chemistry/*metabolism
MH  - Models, Molecular
MH  - Oleic Acid/*metabolism
MH  - Protein Conformation
MH  - Spectrometry, Fluorescence
MH  - Tryptophan/*metabolism
OTO - NOTNLM
OT  - BLA tryptophan
OT  - Bovine alpha-lactalbumin
OT  - Di-8-ANEPPS
OT  - Lipid-protein interaction
OT  - Membrane penetration depth
OT  - REES
EDAT- 2014/05/08 06:00
MHDA- 2014/07/30 06:00
CRDT- 2014/05/08 06:00
PHST- 2014/01/12 00:00 [received]
PHST- 2014/04/27 00:00 [revised]
PHST- 2014/04/28 00:00 [accepted]
PHST- 2014/05/08 06:00 [entrez]
PHST- 2014/05/08 06:00 [pubmed]
PHST- 2014/07/30 06:00 [medline]
AID - S0005-2736(14)00162-X [pii]
AID - 10.1016/j.bbamem.2014.04.027 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2014 Aug;1838(8):2078-86. doi: 
      10.1016/j.bbamem.2014.04.027. Epub 2014 May 4.