Advertisement
J. Lipid Res.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1194/jlr.R800083-JLR200 on November 21, 2008

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
R800083-JLR200v1
50/Supplement/S329    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Small, D. M.
Right arrow Articles by Mitsche, M. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Small, D. M.
Right arrow Articles by Mitsche, M. A.
Related Collections
Right arrow Related Webpages
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Journal of Lipid Research, Vol. 50, S329-S334, April 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Membranes and Lipid Domains

The adsorption of biological peptides and proteins at the oil/water interface. A potentially important but largely unexplored field

Donald M. Small1, Libo Wang and Matthew A. Mitsche

Department of Physiology and Biophysics, Boston University School of Medicine, 700 Albany Street, W-302, Boston, MA 02118

This work is supported in part by Grant NIH-NHLBI 2P01 HL 26335-21.

Published, JLR Papers in Press, November 21, 2008.

1 To whom correspondence should be addressed. e-mail: dmsmall{at}bu.edu


ABSTRACT

This review focuses on some new techniques to study the behavior of peptides and proteins bound to oil droplets. We will show how model peptides e.g., amphipathic {alpha} helices (A{alpha}H) and amphipathic β strand (AβS) and some apolipoproteins adsorb to triacylglycerol (TAG) droplets and how they behave once adsorbed to the interface. While most of the studies described involve peptides and proteins at an oil/water interface, studies can also be carried out when the surface has been partially covered with phospholipids. This work is important because it examines biophysical changes that take place at lipid droplet interfaces and how this may relate to the metabolism of lipoproteins and lipid droplets.

Supplementary key words lipid droplets • oil droplets • fat bodies • adiposomes • obesity • apolipoproteins • surface tension • surface pressure • fat metabolism

Abbreviations: A{alpha}H, Amphipathic {alpha} helices; AβS, Amphipathic β strand; ADRP, adipocite differential related protein; apoA-I, apolipoprotein A-I; apoB, apolipoprotein B; apoC, apolipoprotein C; apoE, apolipoprotein E; CE, cholesterol esters; CPAT, constitutive PAT; CSP, consensus sequence peptide; PAT, Perilipins/ADRP/TIP47; TAG, triacylglycerol; WE, wax esters


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


Related Webpages:

JLR 50th Anniversary Collections
Anniversary Collection::Membranes and Lipid Domains



HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2009 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement