Abstract
The proaduct of catalytic activity of the enzyme phospholipase A2, which resembles the core unit of animal toxins, on phospholipids is a 1:1 mixture of lysolipid and fatty acid. This mixture was studied by time-resolved simultaneous small- and wide angle x-ray diffraction over the temperature range from 23 to 53.5°C An unusually large lamellar structure was observed, with d = 11 nm, contradicting the complex functional dimer model between lysolipid and fatty acid. It can be explained by formation of a "doublebilayer", a new phase consisting of two different bilayers, one formed by lysophospholipid and other by fatty acid, bound together by head group interactions. Its strucutre was confirmed by simulations of the X-ray scattering pattern.
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Funarl, S. S., Rapp, G., & Richter, F. (2009). Double-bilayer: a new phase formed by lysophospholipids and the corresponding fatty acid. Quimica Nova, 32(4), 908–912. https://doi.org/10.1590/s0100-40422009000400015
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