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Biomolecules 2018, 8(3), 45; https://doi.org/10.3390/biom8030045

The Many Faces of Amphipathic Helices

1
Institut Jacques Monod, CNRS, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75013 Paris, France
2
Université Paris-Sud, Université Paris-Saclay, 91405 Orsay, France
3
Université Côte d’Azur, CNRS, IPMC, 06560 Valbonne, France
*
Authors to whom correspondence should be addressed.
Received: 30 May 2018 / Revised: 2 July 2018 / Accepted: 2 July 2018 / Published: 5 July 2018
(This article belongs to the Special Issue Cellular Membrane Domains and Organization)
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Abstract

Amphipathic helices (AHs), a secondary feature found in many proteins, are defined by their structure and by the segregation of hydrophobic and polar residues between two faces of the helix. This segregation allows AHs to adsorb at polar–apolar interfaces such as the lipid surfaces of cellular organelles. Using various examples, we discuss here how variations within this general scheme impart membrane-interacting AHs with different interfacial properties. Among the key parameters are: (i) the size of hydrophobic residues and their density per helical turn; (ii) the nature, the charge, and the distribution of polar residues; and (iii) the length of the AH. Depending on how these parameters are tuned, AHs can deform lipid bilayers, sense membrane curvature, recognize specific lipids, coat lipid droplets, or protect membranes from stress. Via these diverse mechanisms, AHs play important roles in many cellular processes. View Full-Text
Keywords: amphipathic helix; membrane deformation; membrane curvature sensor; ALPS motif; phosphatidic acid; lipid packing defect; perilipin; LEA protein; membrane targeting; desiccation amphipathic helix; membrane deformation; membrane curvature sensor; ALPS motif; phosphatidic acid; lipid packing defect; perilipin; LEA protein; membrane targeting; desiccation
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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Giménez-Andrés, M.; Čopič, A.; Antonny, B. The Many Faces of Amphipathic Helices. Biomolecules 2018, 8, 45.

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