Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1864, Issue 10, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bbamem.2022.184001
Keywords
Helix topology; Antimicrobial peptide; Supported lipid bilayer; MHC II receptor; Hydrophobic mismatch; Magainins; Alamethicin
Categories
Funding
- Agence Nationale de la Recherche [14-CE34-0001-01, InMembrane 15-CE11-0017- 01, 17-CE18-0033-3, 19-AMRB-0004-02, 20-CE18-0021]
- LabEx Chemistry of Complex Systems [10-LABX-0026_CSC]
- CEFIPRA [62T10-1]
- University of Strasbourg
- CNRS
- Region Grand-Est
- RTRA International Center of Frontier Research in Chemistry
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The fatty acyl composition of natural liquid crystalline membranes has significant effects on the structure and activity of membrane proteins, particularly on the transmembrane structure and antimicrobial activity.
Natural liquid crystalline membranes are made up of many different lipids carrying a mixture of saturated and unsaturated fatty acyl chains. Whereas in the past considerable attention has been paid to cholesterol content, the phospholipid head groups and the membrane surface charge the detailed fatty acyl composition was often considered less important. However, recent investigations indicate that the detailed fatty acyl chain composition has pronounced effects on the oligomerization of the transmembrane helical anchoring domains of the MHC II receptor or the membrane alignment of the cationic antimicrobial peptide PGLa. In contrast the antimicrobial peptides magainin 2 and alamethicin are less susceptible to lipid saturation. Using histidine-rich LAH4 designer peptides the high energetic contributions of lipid saturation in stabilizing transmembrane helical alignments are quantitatively evaluated. These observations can have important implications for the biological regulation of membrane proteins and should be taken into considerations during biophysical or structural experiments.
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