High water solubility and fold in amphipols of proteins with large hydrophobic regions: Oleosins and caleosin from seed lipid bodies
type: Dataset
description: Seed lipid bodies constitute natural emulsions stabilized by specialized integral membrane proteins, among which the most abundant are oleosins, followed by the calcium binding caleosin. These proteins exhibit a triblock structure, with a highly hydrophobic central region comprising up to 71 residues. Little is known on their three-dimensional structure. Here we report the solubilization of caleosin and of two oleosins in aqueous solution, using various detergents or original amphiphilic polymers, amphipols. All three proteins, insoluble in water buffers, were maintained soluble either by anionic detergents or amphipols. Neutral detergents were ineffective. In complex with amphipols the oleosins and caleosin contain more beta and less alpha secondary structures than in the SDS detergent, as evaluated by synchrotron radiation circular dichroism. These are the first reported structural results on lipid bodies proteins maintained in solution with amphipols, a promising alternative to notoriously denaturing detergents. (c) 2010 Elsevier B.V. All rights reserved.
landing page: 0005-2736
keyword: amphiphilic-polymer
keyword: caleosin
keyword: corps-dhuile-de-graine
keyword: infoeu-reposemanticsarticle
keyword: journal-articles
keyword: lipid-body
keyword: oleosin
keyword: sdvsalife-sciences-q-bioagricultural-sciences
keyword: secondary-structure
issued: 2026-05-05T09:44:34.224492
modified: 2026-05-05T09:44:34.224498
language: en
contact point: Organization
  fn: CCSD

test_moissonnage_selune
type: Agent

High water solubility and fold in amphipols of proteins with large hydrophobic regions: Oleosins and caleosin from seed lipid bodies
type: Distribution
format: HTML
access URL: https://hal.science/hal-00999885
issued: 2026-05-05T09:44:34.229360
modified: 2026-05-05T09:44:34.211524