Kondrashov, Oleg V.; Kuzmin, Peter I.; Akimov, Sergey A. published the artcile< Hydrophobic Mismatch Controls the Mode of Membrane-Mediated Interactions of Transmembrane Peptides>, Application of C27H44O, the main research area is hydrophobicity transmembrane peptide membrane interaction; lipid membrane; liquid-ordered domain; membrane-mediated interactions; theory of elasticity; transmembrane domain.
Various cellular processes require the concerted cooperative action of proteins. The possibility for such synchronization implies the occurrence of specific long-range interactions between the involved protein participants. Bilayer lipid membranes can mediate protein-protein interactions via relatively long-range elastic deformations induced by the incorporated proteins. We considered the interactions between transmembrane peptides mediated by elastic deformations using the framework of the theory of elasticity of lipid membranes. An effective peptide shape was assumed to be cylindrical, hourglass-like, or barrel-like. The interaction potentials were obtained for membranes of different thicknesses and elastic rigidities. Cylindrically shaped peptides manifest almost neutral average interactions-they attract each other at short distances and repel at large ones, independently of membrane thickness or rigidity. The hourglass-like peptides repel each other in thin bilayers and strongly attract each other in thicker bilayers. On the contrary, the barrel-like peptides repel each other in thick bilayers and attract each other in thinner membranes. These results potentially provide possible mechanisms of control for the mode of protein-protein interactions in membrane domains with different bilayer thicknesses.
Membranes (Basel, Switzerland) published new progress about Bilayer membranes. 434-16-2 belongs to class alcohols-buliding-blocks, and the molecular formula is C27H44O, Application of C27H44O.
Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts