Sorting of Lipidated Peptides in Fluid Bilayers: A Molecular-Level Investigation
Autor: | Paulo F. Almeida, Trevor A. Daly, Steven L. Regen |
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Rok vydání: | 2013 |
Předmět: |
chemistry.chemical_classification
Calorimetry Differential Scanning Chemistry Lipid Bilayers Peripheral membrane protein Monte Carlo method Biophysics Sorting Lipid-anchored protein Context (language use) Peptide General Chemistry Biochemistry Lipids Catalysis Article Partition coefficient Crystallography Colloid and Surface Chemistry Membrane lipids (amino acids peptides and proteins) Lipid bilayer Peptides Monte Carlo Method |
Zdroj: | Biophysical Journal. 104:536a |
ISSN: | 0006-3495 |
DOI: | 10.1016/j.bpj.2012.11.2968 |
Popis: | 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. |
Databáze: | OpenAIRE |
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