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Plos Computational Biology : Lipid Exchange Mechanism of the Cholesteryl Ester Transfer Protein Clarified by Atomistic and Coarsegrained Simulations, Volume 8

By Koivuniemi, Artturi

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Book Id: WPLBN0003941274
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos Computational Biology : Lipid Exchange Mechanism of the Cholesteryl Ester Transfer Protein Clarified by Atomistic and Coarsegrained Simulations, Volume 8  
Author: Koivuniemi, Artturi
Volume: Volume 8
Language: English
Subject: Journals, Science, Computational Biology
Collections: Periodicals: Journal and Magazine Collection (Contemporary), PLoS Computational Biology
Historic
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Publisher: Plos

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Koivuniemi, A. (n.d.). Plos Computational Biology : Lipid Exchange Mechanism of the Cholesteryl Ester Transfer Protein Clarified by Atomistic and Coarsegrained Simulations, Volume 8. Retrieved from http://hawaiilibrary.net/


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Description : Cholesteryl ester transfer protein (CETP) transports cholesteryl esters, triglycerides, and phospholipids between different lipoprotein fractions in blood plasma. The inhibition of CETP has been shown to be a sound strategy to prevent and treat the development of coronary heart disease. We employed molecular dynamics simulations to unravel the mechanisms associated with the CETP-mediated lipid exchange. To this end we used both atomistic and coarse-grained models whose results were consistent with each other. We found CETP to bind to the surface of high density lipoprotein (HDL) -like lipid droplets through its charged and tryptophan residues. Upon binding, CETP rapidly (in about 10 ns) induced the formation of a small hydrophobic patch to the phospholipid surface of the droplet, opening a route from the core of the lipid droplet to the binding pocket of CETP. This was followed by a conformational change of helix X of CETP to an open state, in which we found the accessibility of cholesteryl esters to the C-terminal tunnel opening of CETP to increase. Furthermore, in the absence of helix X, cholesteryl esters rapidly diffused into CETP through the C-terminal opening. The results provide compelling evidence that helix X acts as a lid which conducts lipid exchange by alternating the open and closed states. The findings have potential for the design of novel molecular agents to inhibit the activity of CETP.

 

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