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Sorting of lipidated peptides in fluid bilayers: a molecular-level investigation.

ABSTRACT: Nearest-neighbor recognition (NNR) measurements have been made for two lipidated forms of GlyCys, interacting with analogues of cholesterol and 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) in the liquid-ordered (l(o)) and liquid-disordered (l(d)) phases. Interaction free energies that have been determined from these measurements have been used in Monte Carlo simulations to quantify the distribution of the peptides between liquid-ordered and liquid-disordered regions. These simulations have shown that significant differences in the lipid chains have a very weak influence on the partitioning of the peptide between these two phases. They have also revealed an insensitivity of the peptide partition coefficient, K(p), to the size of the l(o) and l(d) domains that are present. In a broader context, these findings strongly suggest that the sorting of peripheral proteins in cellular membranes via differential lipidation may be more subtle than previously thought.

SUBMITTER: Daly TA

PROVIDER: S-EPMC3474883 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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Sorting of lipidated peptides in fluid bilayers: a molecular-level investigation.

Daly Trevor A TA Almeida Paulo F PF Regen Steven L SL

Journal of the American Chemical Society 20121004 41

Nearest-neighbor recognition (NNR) measurements have been made for two lipidated forms of GlyCys, interacting with analogues of cholesterol and 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) in the liquid-ordered (l(o)) and liquid-disordered (l(d)) phases. Interaction free energies that have been determined from these measurements have been used in Monte Carlo simulations to quantify the distribution of the peptides between liquid-ordered and liquid-disordered regions. These simulations have ...[more]

PMID: 22998217

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