Structure and dynamics of lipid monolayers: Implications for enzyme catalysed lipolysis

Günther H.J. Peters, S. Toxværd, N.B. Larsen, T. Bjørnholm, K. Schaumburg, K. Kjær

    Research output: Contribution to journalJournal articleResearchpeer-review


    We have investigated the role of the substrate on the interfacial activation of Upases by an interdisciplinary study of the structure and dynamics of 1,2-sn dipalmitoylglycerol monolayers at distinct surface pressures. The diglyceride Langmuir film undergoes two phase transitions occurring at 38.3 and 39.8 Å2 per molecule. The first transition is unique for diglyceride molecules and is driven by a reorganization of the headgroups causing a change in the hydrophobicity of the oil-water interface. X-ray diffraction studies of different mesophases shows that in the two highest pressure phases, the alkyl chains pack in an hexagonal structure relaxing to a distorted-hexagonal lattice in the lowest pressure phase with the alkyl chains tilted by approx 14° in a direction close to a nearest neighbour direction.
    Original languageEnglish
    JournalNature Structural Biology
    Pages (from-to)395-401
    Number of pages7
    Publication statusPublished - 1995


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