title: The role of chain rigidity in lipid self-association: comparative study of dihexanoyl- and disorbyl-phosphatidylcholines.
abstract: In the course of structure-function investigations of lipids a phosphatidylcholine molecule with short and rigid tails, di-2,4-hexadienoylphosphatidylcholine (DiSorbPC), was synthesized and studied in comparison with its saturated analog, dihexanoylphosphatidylcholine (DHPC). Conjugated double bonds in the acyl chains in DiSorbPC reduce considerably the number of possible conformers of the lipid within an aggregate. This leads to impaired packing of unsaturated acyl chains and thus, to a surprisingly high (115 Å(2)) area per molecule for DiSorbPC at the air-water interface and failure to form micelles of regular size and shape. Details on DiSorbPC aggregation and packing provided by a set of experimental techniques combined with molecular dynamics simulations are presented.
authors.affiliation: Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, Moscow, Russia.
authors.forename: A A
authors.initials: AA
authors.lastname: Semenova
authors.forename: A O
authors.initials: AO
authors.lastname: Chugunov
authors.forename: P V
authors.initials: PV
authors.lastname: Dubovskii
authors.forename: V V
authors.initials: VV
authors.lastname: Chupin
authors.forename: P E
authors.initials: PE
authors.lastname: Volynsky
authors.forename: I A
authors.initials: IA
authors.lastname: Boldyrev
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D008823:Micelles; D056004:Molecular Dynamics Simulation; D010713:Phosphatidylcholines / Q000737:chemistry*; D013500:Surface Tension
chemical_list: D008823:Micelles; D010713:Phosphatidylcholines; C032166:1,2-hexanoylphosphatidylcholine