Lipid Binding of the Exchangeable Apolipoprotein Apolipophorin III Induces Major Changes in Fluorescence Properties of Tryptophans 115 and 130†

Biochemistry ◽  
2000 ◽  
Vol 39 (23) ◽  
pp. 6874-6880 ◽  
Author(s):  
Paul M. M. Weers ◽  
Elmar J. Prenner ◽  
Cyril Kay ◽  
Robert O. Ryan
Keyword(s):  
Lipid Binding ◽  
Fluorescence Properties ◽  
Apolipophorin Iii ◽  
Exchangeable Apolipoprotein

scholarly journals Role of the N- and C-Terminal Helices in Apolipophorin III Stability and Lipid Binding

2012 ◽  
Vol 102 (3) ◽  
pp. 58a
Author(s):  
Pankaj Dwivedi ◽  
Johana Rodriguez ◽  
Paul M.M. Weers
Keyword(s):  
Lipid Binding ◽  
Apolipophorin Iii

Role of charged amino acid side chains in the stability and lipid binding ofManduca sexta apolipophorin III

1995 ◽  
Vol 30 (2-3) ◽  
pp. 211-223 ◽  
Author(s):  
Minal Upadhyaya ◽  
Kim Oikawa ◽  
Cyril M. Kay ◽  
Douglas G. Scraba ◽  
Roger Bradley ◽  
...  
Keyword(s):  
Amino Acid ◽  
Lipid Binding ◽  
Side Chains ◽  
Apolipophorin Iii ◽  
Amino Acid Side Chains ◽  
The Stability

Spectroscopic and Lipid Binding Studies on the Amino and Carboxyl Terminal Fragments of Locusta migratoria Apolipophorin III

Biochemistry ◽  
1995 ◽  
Vol 34 (37) ◽  
pp. 11822-11830 ◽  
Author(s):  
Vasanthy Narayanaswami ◽  
Paul M. M. Weers ◽  
Jan Bogerd ◽  
Frank P. Kooiman ◽  
Cyril M. Kay ◽  
...  
Keyword(s):  
Locusta Migratoria ◽  
Lipid Binding ◽  
Binding Studies ◽  
Apolipophorin Iii ◽  
Carboxyl Terminal

Abstract 391: Apolipoprotein E3, Apolipoprotein AI, and Apolipophorin III Chimeras Provide Insight Into the Domain Organization of Apolipoproteins

2016 ◽  
Vol 36 (suppl_1) ◽  
Author(s):  
James V Horn ◽  
Mark Lek ◽  
Nnejiuwa Ibe ◽  
Rachel A Ellena ◽  
Wendy H Beck ◽  
...  
Keyword(s):  
Cholesterol Efflux ◽  
Dominant Role ◽  
Lipoprotein Metabolism ◽  
Lipid Binding ◽  
Binding Activity ◽  
Domain Model ◽  
Helix Bundle ◽  
Apolipophorin Iii ◽  
Helical Content ◽  
The Stability

Apolipoproteins (apo) A-I and E are exchangeable apolipoproteins that play a dominant role in regulating lipoprotein metabolism. They are composed of a series of amphipathic α-helices, which are organized into an N-terminal (NT) helix bundle domain and a smaller C-terminal (CT) domain. The objective of the current study is to understand the functional and structural role of the domains of these proteins by “domain swapping” using apoE3 and apoAI, both of which bear a 4-helix bundle in their NT domain, and apolipophorin III (apoLp-III), a monomeric one-domain model apolipoprotein. A series of chimeric apolipoproteins were generate: apoE3-NT/apoAI-CT, apoAI-NT/apoE-CT and apoLp-III/apoA-I-CT. The α-helical content of the chimeras was comparable to that of the parent proteins. Unfolding studies indicated that addition of CT-apoE3 to NT-apoAI conferred more stability to apoAI. While addition of CT-apoAI to NT-apoE3 had no significant effect on the stability of apoE3, addition of NT-apoAI to apoLp-III increased the stability of apoLp-III. Moreover, apoLp-III switched from a monomeric to an oligomeric protein upon addition of CT-apoAI, showing that CT-apoAI has a strong tendency to self-associate. Addition of CT-apoAI to NT-apoE or apoLp-III increased the lipid binding activity by ~ 10-fold, while addition of apoE-CT to apoA-I-NT had no measurable effect on the lipid binding activity. All three chimeras promote ABCA1-mediated cholesterol efflux from J774 macrophages, with the efflux capability being highest for apoAI-NT/apoE-CT. Whereas apoE3-NT/apoAI-CT elicits LDLr binding ability, apoAI-NT/apoE-CT did not. These results suggest that CT of apoAI is a strong promoter of lipid binding, while CT of apoE3 can improve cholesterol efflux ability of apoAI.

An N-Terminal Three-Helix Fragment of the Exchangeable Insect Apolipoprotein Apolipophorin III Conserves the Lipid Binding Properties of Wild-Type Protein†

Biochemistry ◽  
2001 ◽  
Vol 40 (10) ◽  
pp. 3150-3157 ◽  
Author(s):  
Matthias Dettloff ◽  
Paul M. M. Weers ◽  
Marc Niere ◽  
Cyril M. Kay ◽  
Robert O. Ryan ◽  
...  
Keyword(s):  
Lipid Binding ◽  
Wild Type ◽  
Binding Properties ◽  
Apolipophorin Iii ◽  
Type Protein ◽  
Wild Type Protein
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