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Further observations on cord-inducing factor.

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D S GOLDMAN, D G ANDERSON, E C GOLDMAN. 1959. Further observations on cord-inducing factor.. https://doi.org/10.1128/jb.77.1.121-122.1959

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Molecular packing of cord factor and its interaction with phosphatidylinositol in mixed monolayers.

Cord factor (trehalose 6,6'-dimycolate, CF) is a glycolipid located in the outer mycobacterial cell wall that is implicated in the pathogenesis of mycobacteria. Furthermore, CF is a convenient model for studying mycolic acid residues, the major lipid constituents of the mycobacterial cell wall that are believed to form a barrier against drug penetration. The surface properties of CF and its interactions with phosphatidylinositol (PI) have been investigated using the monolayer technique. During compression/expansion/recompression cycles, CF monolayers switch from a loosely packed to a more tightly packed structure. The change in surface properties suggests a molecular rearrangement, perhaps involving interdigitation of long and short chains of the CF molecules. In CF-PI monolayers, maximal lateral packing density occurs between 0.5 and 0.7 mole fraction CF, which is close to the relative composition of mycolic acid residues and shorter-chain lipids in the mycobacterial cell wall. Low concentrations of CF increase the order in PI monolayers, consistent with CF toxicity involving rigidification of cell membranes.

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Characterization of the trehalose 6,6'-dimycolate surface monolayer by scanning tunneling microscopy.

The toxicity of trehalose 6,6'-dimycolate (TDM), a glycolipid of mycobacteria, requires presentation as a surface monolayer. Our model of the structure of the TDM monolayer was confirmed and extended by scanning tunneling microscopy. It consists of linear arrays with a periodicity of approximately 90 A (9 nm) that clustered in groups of four to form secondary structures with a periodicity of 360 A (36 nm).

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