[HTML][HTML] Lipid binding-induced conformational change in human apolipoprotein E: evidence for two lipid-bound states on spherical particles
H Saito, P Dhanasekaran, F Baldwin… - Journal of Biological …, 2001 - ASBMB
Apolipoprotein (apo) E contains two structural domains, a 22-kDa (amino acids 1–191) N-
terminal domain and a 10-kDa (amino acids 223–299) C-terminal domain. To better
understand apoE-lipid interactions on lipoprotein surfaces, we determined the
thermodynamic parameters for binding of apoE4 and its 22-and 10-kDa fragments to triolein-
egg phosphatidylcholine emulsions using a centrifugation assay and titration calorimetry. In
both large (120 nm) and small (35 nm) emulsion particles, the binding affinities decreased in …
terminal domain and a 10-kDa (amino acids 223–299) C-terminal domain. To better
understand apoE-lipid interactions on lipoprotein surfaces, we determined the
thermodynamic parameters for binding of apoE4 and its 22-and 10-kDa fragments to triolein-
egg phosphatidylcholine emulsions using a centrifugation assay and titration calorimetry. In
both large (120 nm) and small (35 nm) emulsion particles, the binding affinities decreased in …