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 (AalphaH) and amphipathic beta strand (AbetaS) 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.

Highlights

  • This review focuses on some new techniques to study the behavior of peptides and proteins bound to oil droplets

  • This review centers on some new methods which can be used to study the physical properties of proteins which bind to lipid droplets [1,2,3,4,5]

  • All of these lipid droplets are emulsions consisting of a core of one or more very hydrophobic lipids including triacylglycerol (TAG), wax esters (WE), cholesterol esters (CE), retinal esters,and poly(hydroxyalkanoates) [6]

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Summary

PROTEINS ASSOCIATED WITH LIPID DROPLETS

The great interest in obesity and its control has stimulated new research on the metabolism of fat, its storage, its hydrolysis and usage, and more recently, on the nature of lipid droplets in cells [6, 7, 12,13,14,15]. Oleosin consists of N- and C-terminal charged amphipathic a helices (AaH) domains that lie on the surface of the droplet and a central ?60aa hydrophobic b sheet that penetrates into the core lipid. TAG rich chylomicrons and very low density lipoproteins (VLDL) are other forms of emulsion particles that are generated in the intestines and liver, respectively [20, 21] Budding of these nascent particles occur from the endoplasmic reticulum into the lumen [22] and after some modifications they are secreted into plasma [21]. As VLDL is metabolized it loses most of its TAG, phospholipids and exchangeable apolipoproteins and it becomes much smaller and enriched in CE This end product is called low density lipoprotein (LDL) and the only protein it contains is apolipoprotein. While it is certain that apoB interacts with the core lipid in LDL, it has not been established in VLDL or chylomicrons that apoB interacts directly with the core but we suggest that some domains do interact with core TAG [24]

BIOSYNTHESIS OF LIPID DROPLETS
STUDYING THE BINDING OF PEPTIDES TO LIPID DROPLETS
Findings
Larger complex peptides and native proteins
Full Text
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