Many length scales surface fractality in monomolecular films of whole myelin lipids and proteins.

RAFAEL GUSTAVO OLIVEIRA; TANAKA, M.; MAGGIO, B.

JOURNAL OF STRUCTURAL BIOLOGY

Academic Press Inc.

Año: 2005 vol. 149 p. 158 - 158

1047-8477

onomolecular films prepared with all the lipid and protein components of myelin were spread at the air/aqueous buffer interface from isolated bovine spinal cord myelin fully dissolved in chloroform:methanol (2:1) or by surface free energy shock of myelin membrane microvesicles. These monolayers show indistinguishable surface behavior, with similar compositional phase coexistence through all the compression isotherm on several subphase conditions. The domains were observed through epifluorescence and Brewster angle microscopy on the air/water interface and on Langmuir?Blodgett films. Their thickness was measured ellipsometrically. Under  molecular packing conditions resembling those found in the natural membrane, the morphology and size of the domains are highly self-similar, displaying no  characteristic length scale. These properties are the hallmark of fractal objects. The fractality extends at least three orders of magnitudes, from the micrometer to the millimeter range, the fracta