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

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

doi:10.1038/srep08741

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

Journal Article · Wed Mar 04 00:00:00 EST 2015 · Scientific Reports

DOI:https://doi.org/10.1038/srep08741· OSTI ID:1190957

Zhang, Meng ^[1]; Charles, River ^[1]; Tong, Huimin ^[1]; Zhang, Lei ^[1]; Patel, Mili ^[2]; Wang, Francis ^[1]; Rames, Matthew J. ^[1]; Ren, Amy ^[1]; Rye, Kerry-Anne ^[2]; Qiu, Xiayang ^[3]; Johns, Douglas G. ^[4]; Charles, M. Arthur ^[5]; Ren, Gang ^[1]

Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
University of New South Wales, Kensington, Sydney (Australia). Centre for Vascular Research.
Pfizer, Inc., Groton, CT (United States)
Merck Research Labs., Rahway, NJ (United States)
University of California, San Francisco, CA (United States). School of Medicine.

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.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1190957

Alternate ID(s):: OSTI ID: 1407290

Journal Information:: Scientific Reports, Vol. 5, Issue 3; ISSN 2045-2322

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 33 works

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