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© Research
Publication : International journal of biological macromolecules

Targeting structural flexibility in low density lipoprotein by integrating cryo-electron microscopy and high-speed atomic force microscopy.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in International journal of biological macromolecules - 22 Aug 2023

Cisse A, Desfosses A, Stainer S, Kandiah E, Traore DAK, Bezault A, Schachner-Nedherer AL, Leitinger G, Hoerl G, Hinterdorfer P, Gutsche I, Prassl R, Peters J, Kornmueller K

Link to Pubmed [PMID] – 37619685

Link to DOI – 10.1016/j.ijbiomac.2023.126345

Int J Biol Macromol 2023 Aug; 252(): 126345

Low-density lipoprotein (LDL) plays a crucial role in cholesterol metabolism. Responsible for cholesterol transport from the liver to the organs, LDL accumulation in the arteries is a primary cause of cardiovascular diseases, such as atherosclerosis. This work focuses on the fundamental question of the LDL molecular structure, as well as the topology and molecular motions of apolipoprotein B-100 (apo B-100), which is addressed by single-particle cryo-electron microscopy (cryo-EM) and high-speed atomic force microscopy (HS-AFM). Our results suggest a revised model of the LDL core organization with respect to the cholesterol ester (CE) arrangement. In addition, a high-density region close to the flattened poles could be identified, likely enriched in free cholesterol. The most remarkable new details are two protrusions on the LDL surface, attributed to the protein apo B-100. HS-AFM adds the dimension of time and reveals for the first time a highly dynamic direct description of LDL, where we could follow large domain fluctuations of the protrusions in real time. To tackle the inherent flexibility and heterogeneity of LDL, the cryo-EM maps are further assessed by 3D variability analysis. Our study gives a detailed explanation how to approach the intrinsic flexibility of a complex system comprising lipids and protein.