Acyl-coenzyme A organizes laterally in membranes and is recognized specifically by acyl-coenzyme A binding protein

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Long chain acyl-coenzyme A (acyl-CoA) is a biochemically important amphiphilic molecule that is known to partition strongly into membranes by insertion of the acyl chain. At present, microscopically resolved evidence is lacking on how acyl-CoA influences and organizes laterally in membranes. By atomic force microscopy (AFM) imaging of membranes exposed to acyl-CoA in μM concentrations, it is shown that aggregate formation takes place within the membrane upon long-time exposure. It is known that acyl-CoA is bound by acyl-CoA binding protein (ACBP) with high affinity and specificity and that ACBP may bind and desorb membrane-bound acyl-CoA via a partly unknown mechanism. Following incubation with acyl-CoA, it is shown that ACBP is able to reverse the formation of acyl-CoA aggregates and to associate peripherally with acyl-CoA on the membrane surface. Our microscopic results point to the role of ACBP as an intermembrane transporter of acyl-CoA and demonstrate the ability of AFM to reveal the remodelling of membranes by surfactants and proteins.

Original languageEnglish
JournalFEBS Letters
Issue number2-3
Pages (from-to)253-258
Number of pages6
Publication statusPublished - 25 Sep 2003

    Research areas

  • Acyl-coenzyme A binding protein, Atomic force microscopy, Lipid bilayer membrane, Long chain fatty acyl-coenzyme A, Phosphatidylcholine

ID: 230986143