Many length scales surface fractality in monomolecular films of whole myelin lipids and proteins.
Monomolecular 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 fractal dimension being about 1.7. A possible implication of fractality in membrane structure and/or function is demonstrated through the high fluctuation of the propagation of signals through constrained diffusion in corrals formed by domains in the plane of the monolayer, which restricts the diffusion of a fluorescent probe over many length scale domains.
Oliveira
Rafael G
RG
Departamento de Química Biológica-CIQUIBIC, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, 5000 Córdoba, Argentina.
Tanaka
Motomu
M
Maggio
Bruno
B
D000818:Animals; D002417:Cattle; D017709:Fractals; D008563:Membrane Lipids / Q000737:chemistry*; D008856:Microscopy, Fluorescence; D009185:Myelin Proteins / Q000737:chemistry*; D009186:Myelin Sheath / Q000737:chemistry*; D013116:Spinal Cord / Q000737:chemistry; D013499:Surface Properties
D008563:Membrane Lipids; D009185:Myelin Proteins