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Title: HDL surface lipids mediate CETP binding as revealed by electron microscopy and molecular dynamics simulation

Abstract

Cholesteryl ester transfer protein (CETP) mediates the transfer of cholesterol esters (CE) from atheroprotective high-density lipoproteins (HDL) to atherogenic low-density lipoproteins (LDL). CETP inhibition has been regarded as a promising strategy for increasing HDL levels and subsequently reducing the risk of cardiovascular diseases (CVD). Although the crystal structure of CETP is known, little is known regarding how CETP binds to HDL. Here, we investigated how various HDL-like particles interact with CETP by electron microscopy and molecular dynamics simulations. Results showed that CETP binds to HDL via hydrophobic interactions rather than protein-protein interactions. The HDL surface lipid curvature generates a hydrophobic environment, leading to CETP hydrophobic distal end interaction. This interaction is independent of other HDL components, such as apolipoproteins, cholesteryl esters and triglycerides. Thus, disrupting these hydrophobic interactions could be a new therapeutic strategy for attenuating the interaction of CETP with HDL.

Authors:
 [1];  [1];  [1];  [1];  [2];  [1];  [1];  [1];  [2];  [3];  [4];  [5];  [1]
+ Show Author Affiliations
  1. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  2. University of New South Wales, Kensington, Sydney (Australia). Centre for Vascular Research.
  3. Pfizer, Inc., Groton, CT (United States)
  4. Merck Research Labs., Rahway, NJ (United States)
  5. University of California, San Francisco, CA (United States). School of Medicine.
Publication Date:
Research Org.:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH)
OSTI Identifier:
1190957
Alternate Identifier(s):
OSTI ID: 1407290
Grant/Contract Number:  
AC02-05CH11231
Resource Type:
Accepted Manuscript
Journal Name:
Scientific Reports
Additional Journal Information:
Journal Volume: 5; Journal Issue: 3; Journal ID: ISSN 2045-2322
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Zhang, Meng, Charles, River, Tong, Huimin, Zhang, Lei, Patel, Mili, Wang, Francis, Rames, Matthew J., Ren, Amy, Rye, Kerry-Anne, Qiu, Xiayang, Johns, Douglas G., Charles, M. Arthur, and Ren, Gang. HDL surface lipids mediate CETP binding as revealed by electron microscopy and molecular dynamics simulation. United States: N. p., 2015. Web. doi:10.1038/srep08741.
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Zhang, Meng, Charles, River, Tong, Huimin, Zhang, Lei, Patel, Mili, Wang, Francis, Rames, Matthew J., Ren, Amy, Rye, Kerry-Anne, Qiu, Xiayang, Johns, Douglas G., Charles, M. Arthur, & Ren, Gang. HDL surface lipids mediate CETP binding as revealed by electron microscopy and molecular dynamics simulation. United States. https://doi.org/10.1038/srep08741
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Zhang, Meng, Charles, River, Tong, Huimin, Zhang, Lei, Patel, Mili, Wang, Francis, Rames, Matthew J., Ren, Amy, Rye, Kerry-Anne, Qiu, Xiayang, Johns, Douglas G., Charles, M. Arthur, and Ren, Gang. Wed . "HDL surface lipids mediate CETP binding as revealed by electron microscopy and molecular dynamics simulation". United States. https://doi.org/10.1038/srep08741. https://www.osti.gov/servlets/purl/1190957.
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@article{osti_1190957,
title = {HDL surface lipids mediate CETP binding as revealed by electron microscopy and molecular dynamics simulation},
author = {Zhang, Meng and Charles, River and Tong, Huimin and Zhang, Lei and Patel, Mili and Wang, Francis and Rames, Matthew J. and Ren, Amy and Rye, Kerry-Anne and Qiu, Xiayang and Johns, Douglas G. and Charles, M. Arthur and Ren, Gang},
abstractNote = {Cholesteryl ester transfer protein (CETP) mediates the transfer of cholesterol esters (CE) from atheroprotective high-density lipoproteins (HDL) to atherogenic low-density lipoproteins (LDL). CETP inhibition has been regarded as a promising strategy for increasing HDL levels and subsequently reducing the risk of cardiovascular diseases (CVD). Although the crystal structure of CETP is known, little is known regarding how CETP binds to HDL. Here, we investigated how various HDL-like particles interact with CETP by electron microscopy and molecular dynamics simulations. Results showed that CETP binds to HDL via hydrophobic interactions rather than protein-protein interactions. The HDL surface lipid curvature generates a hydrophobic environment, leading to CETP hydrophobic distal end interaction. This interaction is independent of other HDL components, such as apolipoproteins, cholesteryl esters and triglycerides. Thus, disrupting these hydrophobic interactions could be a new therapeutic strategy for attenuating the interaction of CETP with HDL.},
doi = {10.1038/srep08741},
journal = {Scientific Reports},
number = 3,
volume = 5,
place = {United States},
year = {Wed Mar 04 00:00:00 EST 2015},
month = {Wed Mar 04 00:00:00 EST 2015}
}
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https://doi.org/10.1038/srep08741
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Safety and Tolerability of Dalcetrapib††Conflicts of interest: Dr. Stein has received grants for studies of lipid-modifying agents, has received consulting fees and honoraria for professional input regarding agents to modify lipid profile, and/or has delivered lectures for the American Association for Clinical Chemistry, Washington, District of Columbia; Abbott Laboratories, Abbott Park, Illinois; AstraZeneca, Wilmington, Delaware; the United States Food and Drug Administration, Washington, District of Columbia; F. Hoffmann-La Roche Ltd., Basel, Switzerland; Isis Pharmaceuticals, Inc., Carlsbad, California; Merck & Co., Whitehouse Station, New Jersey; the National Lipid Association, Jacksonville, Florida; Novartis International AG, Basel Switzerland; Reliant Pharmaceuticals, Inc., Liberty Corner, New Jersey; Daiichi Sankyo Co., Ltd., Tokyo, Japan; Schering-Plough Corporation, Kenilworth, New Jersey; Takeda Pharmaceutical Company Ltd., Osaka, Japan; and Wyeth, Madison, New Jersey. Dr. Stroes has received consulting fees and honoraria from F. Hoffmann-La Roche Ltd. and Novartis International AG. Dr. Steiner has received consulting fees and honoraria from F. Hoffmann-La Roche Ltd.; Solvay, Brussels, Belgium; Ethypharm S.A., Saint-Cloud, France; and Merck Frosst Canada Ltd. (Kirkland, Quebec, Canada)/Schering-Plough Corporation. Dr. Buckley has received research grants from AstraZeneca; Merck Sharp & Dohme, Dublin, Ireland; and Pfizer, Inc., New York, New York. Dr. Buckley has received honoraria and consulting fees and/or delivered lectures for AstraZeneca; Bristol-Myers Squibb, New York, New York; F. Hoffmann-La Roche Ltd.; Novartis International AG; Pfizer, Inc.; and Sanofi-Aventis, Paris, France. Dr. Capponi has received consulting fees and honoraria from F. Hoffmann-La Roche Ltd. Dr. Burgess is an employee of Hoffmann-La Roche Inc., Nutley, New Jersey. Drs. Niesor and Kallend are employees of F. Hoffmann-La Roche Ltd. Dr. Kastelein has received research grants, honoraria, or consulting fees for professional input and/or has delivered lectures for Pfizer, Inc.; Merck Sharp & Dohme; F. Hoffmann-La Roche Ltd.; Novartis International AG; Isis Pharmaceuticals, Inc.; Kowa Pharmaceutical Company Ltd., Nagoya, Japan; Schering-Plough Corporation; and AstraZeneca.
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