The interaction of apoA-I from human high density lipoprotein with lysolecithin.
The binding of apoA-I to lysolecithin has been studied by fluorescence and circular dichroism. The influence of the conformation of apoA-I on its interaction with lysolecithin has also been evaluated. ApoA-I is bound to lysolecithin with an association greater than 10(7) whether apoA-I is native or highly unfolded in 1.8 M guanidinium hydrochloride. The association of apoA-I with lysolecithin results in an increase in secondary structure. A 25-residue fragment of apoA-I binds to lysolecithin equally strongly as the native molecule.
D001059:Apoproteins / Q000097:blood; D001665:Binding Sites; D002942:Circular Dichroism; D006146:Guanidines; D006801:Humans; D007700:Kinetics; D008075:Lipoproteins, HDL / Q000097:blood*; D008244:Lysophosphatidylcholines; D008433:Mathematics; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013386:Succinates
D001059:Apoproteins; D006146:Guanidines; D008075:Lipoproteins, HDL; D008244:Lysophosphatidylcholines; D013386:Succinates