Next Article in Journal
ENABLE 2017, the First European PhD and Post-Doc Symposium. Session 1: Building the Foundations of Biology: Synthetic and Cellular Research
Next Article in Special Issue
Ectopic Neo-Formed Intracellular Membranes in Escherichia coli: A Response to Membrane Protein-Induced Stress Involving Membrane Curvature and Domains
Previous Article in Journal
A Review of the Recent Advances Made with SIRT6 and its Implications on Aging Related Processes, Major Human Diseases, and Possible Therapeutic Targets
Previous Article in Special Issue
Anandamide Revisited: How Cholesterol and Ceramides Control Receptor-Dependent and Receptor-Independent Signal Transmission Pathways of a Lipid Neurotransmitter
Review

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

Graphical abstract

MDPI and ACS Style

Giménez-Andrés, M.; Čopič, A.; Antonny, B. The Many Faces of Amphipathic Helices. Biomolecules 2018, 8, 45. https://doi.org/10.3390/biom8030045

AMA Style

Giménez-Andrés M, Čopič A, Antonny B. The Many Faces of Amphipathic Helices. Biomolecules. 2018; 8(3):45. https://doi.org/10.3390/biom8030045

Chicago/Turabian Style

Giménez-Andrés, Manuel; Čopič, Alenka; Antonny, Bruno. 2018. "The Many Faces of Amphipathic Helices" Biomolecules 8, no. 3: 45. https://doi.org/10.3390/biom8030045

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop