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University of Illinois at Urbana-Champaign

Interaction of Human Apolipoprotein a-I With Dipalmitoyl Phosphatidylcholine

Abstract

dc:description

Dipalmitoylphosphatidylcholine (DPPC) bilayer lipid will react with human apolipoprotein A-I (apo A-I) to form lipid-protein micellar complexes. The reactivity of the lipid bilayer is dependent upon the physical state of the vesicle. Large vesicles with essentially planar bilayers do not form complexes except at temperatures near the gel to liquid-crystalline phase transition of the vesicles where they demonstrate a slow rate of complex formation. Small unilamellar vesicles which contain bilayers with a high degree of surface curvature are rapidly incorporated into micellar complexes at temperatures near and above the transition temperature. The highly reactive nature of the small vesicles is explained by the marked curvature of the lipid bilayer which affects the packing of the DPPC molecules in the bilayer and facilitate its penetration by apo A-I.

Degree

thesis:*
Name thesis:degree_name
Ph.D.
Level thesis:degree_level
Dissertation
Discipline thesis:degree_discipline
Biochemistry
Grantor
University of Illinois at Urbana-Champaign
Year dc:date
2014

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Wetterau, John Rowley, Ii

Subjects

dc:subject × 1

Identifiers

dc:identifier.*
Identifier
(UMI)AAI8303021
OAI identifier oai:identifier
oai:www.ideals.illinois.edu:2142/70515

Chain of custody

source
Harvested from
University of Illinois - Urbana-Champaign
Base URL
www.ideals.illinois.edu/oai-pmh
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Wetterau, John Rowley, Ii. Interaction of Human Apolipoprotein a-I With Dipalmitoyl Phosphatidylcholine. Dissertation thesis, University of Illinois at Urbana-Champaign, 2014. http://hdl.handle.net/2142/70515