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• W2950854413 abstract "Because of its critical role in high density lipoprotein (HDL) metabolism, significant work has been devoted to studying apolipoprotein (apo)A-I structure in its lipid-bound state, particularly reconstituted forms of HDL (rHDL). Unfortunately, high-resolution structural studies have not been successful because of HDL heterogeneity and compositional dynamics. There is general agreement that apoA-I adopts an antiparallel arrangement on rHDL with the majority of the molecule conforming to the “double belt” model. However, less is understood about the locations of the N- and C-termini in these particles. The classic double belt predicts that, in a particle containing two molecules of apoA-I, all four termini are localized to one area of the particle. However, other models predict that they are far apart. To address this issue, we generated a series of covalently connected apoA-I dimers and tested their ability to generate rHDL particles. The dimeric (d)-apoA-I C-N mutant, locked the C-terminus of one apoA-I molecule to the N-terminus of a second molecule with three intervening Ala residues. Linked by strategically introduced cysteine residues, the d-apoA-I C-C , and d-apoA-I N-N mutants lock the C-termini and the N-termini of two apoA-I molecules together, respectively. When all three of these mutants were reconstituted into rHDL particles using sodium cholate and synthetic phospholipids, the resulting particles closely resembled those generated with wild-type (WT) apoA-I. This indicates a ring-like structure predicted by the double belt. However, when testing the ability of these mutants to spontaneously clear lipid, we found that both the N- and C- termini required the ability to separate and move independently to form normal particles. Native gel analysis showed the dimerized lipid-free mutants present as a tight homogenous band compared to wild-type which runs as a mixture of oligomers. We are currently evaluating if the homogeneity of these mutants can allow for more facile crystallization of full-length apoA-I. Further studies with these stabilized mutants should help us understand the structural basis underlying HDL’s diverse functions, which is essential for developing HDL-based therapies for cardiovascular disease." @default.
• W2950854413 created "2019-06-27" @default.
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• W2950854413 date "2016-05-01" @default.
• W2950854413 modified "2023-09-26" @default.
• W2950854413 title "Abstract 393: Covalently Connected Apolipoprotein A-I Molecules Provide Support for the Double Belt Model in Reconstituted HDL" @default.
• W2950854413 doi "https://doi.org/10.1161/atvb.36.suppl_1.393" @default.
• W2950854413 hasPublicationYear "2016" @default.
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