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

Abstract:

: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.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Almog R,Mannella CA

doi

10.1016/S0006-3495(96)79523-1

subject

Has Abstract

pub_date

1996-12-01 00:00:00

pages

3311-9

issue

6

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(96)79523-1

journal_volume

71

pub_type

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