Mechanism of lipid-protein interaction in the plasma lipoproteins: relationship of lipid-binding sites to antigenic sites in apolipoprotein A-II

Biochemistry ◽  
1979 ◽  
Vol 18 (18) ◽  
pp. 3984-3988 ◽  
Author(s):  
Simon J. T. Mao ◽  
James T. Sparrow ◽  
Antonio M. Gotto ◽  
Richard L. Jackson
Keyword(s):  
Protein Interaction ◽  
Binding Sites ◽  
Lipid Binding ◽  
Plasma Lipoproteins ◽  
Apolipoprotein A ◽  
Antigenic Sites ◽  
Lipid Protein Interaction ◽  
Relationship Of

Mechanism of lipid-protein interaction in the plasma lipoproteins: lipid-binding properties of synthetic fragments of apolipoprotein A-II

Biochemistry ◽  
1977 ◽  
Vol 16 (19) ◽  
pp. 4150-4156 ◽  
Author(s):  
S. J. T. Mao ◽  
J. T. Sparrow ◽  
E. B. Gilliam ◽  
A. M. Gotto ◽  
R. L. Jackson
Keyword(s):  
Protein Interaction ◽  
Lipid Binding ◽  
Plasma Lipoproteins ◽  
Binding Properties ◽  
Apolipoprotein A ◽  
Lipid Protein Interaction

scholarly journals Structure-function studies of apoA-I variants

2002 ◽  
Vol 43 (8) ◽  
pp. 1283-1292 ◽  
Author(s):  
Dmitri Sviridov ◽  
Anh Hoang ◽  
Wei Huang ◽  
Jun Sasaki
Keyword(s):  
Central Region ◽  
Binding Sites ◽  
Cholesterol Efflux ◽  
Lipid Binding ◽  
Binding Properties ◽  
Apolipoprotein A ◽  
Self Association ◽  
Rate Limiting ◽  
Lower Capacity ◽  
Combined Data

Five mutants of apolipoprotein A-I (apoA-I), apoA-I(Δ63–73), apoA-I(Δ140–150), apoA-I(63–73@140–150), apoA-I(R149V), and apoA-I(P143A) were compared with human plasma apoA-I for their ability to promote cholesterol and phospholipid efflux from HepG2 cells. A significantly lower capacity to promote cholesterol and phospholipid efflux was observed with lipid-free apoA-I(Δ63–73), while mutations apoA-I(Δ140–150) and apoA-I(P143A) affected phospholipid efflux only. When added as apoA-I/palmitoyloleoyl phosphatidylcholine (POPC) complex, mutations apoA-I(63–73@140–150) and apoA-I(Δ140–150) affected cholesterol efflux. None of the mutations affected α-helicity of the lipid-free mutants or their self-association. Five natural mutations of apoA-I, apoA-I(A95D), apoA-I (Y100H), apoA-I(E110K), apoA-I(V156E), and apoA-I (H162Q) were studied for their ability to bind lipids and promote cholesterol efflux. None of the mutations affected lipid-binding properties, cholesterol efflux, or α-helicity of lipid-free mutants. Two mutations affected self-association of apoA-I: apoA-I(A95D) was more prone to self-association, while apoA-I(E100H) did not self-associate.The following conclusions could be made from the combined data: i) regions 210–243 and 63–100 are the lipid-binding sites of apoA-I and are also required for the efflux of lipids to lipid-free apoA-I, suggesting that initial lipidation of apoA-I is rate limiting in efflux; ii) in addition to the lipid-binding regions, the central region is important for cholesterol efflux to lipidated apoA-I, suggesting its possible involvement in interaction with cells.

Preparation of Chloroplast Lipid Membrane and Lipid-protein Interaction Assay

BIO-PROTOCOL ◽  
2016 ◽  
Vol 6 (3) ◽  
Author(s):  
Kumiko Okazaki ◽  
Shin-ya Miyagishima ◽  
Hajime Wada
Keyword(s):  
Protein Interaction ◽  
Lipid Membrane ◽  
Lipid Protein Interaction
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