Interaction of synthetic peptide corresponding to signal sequence of glucitol permease of Escherichia coli and its analogue with liposomes.
The N-terminal signal sequence of glucitol permease of Escherichia Coli (Gut22) and its analogue (Gut22Ana) were synthesized. The analogue had a Pro residue substituting for the His at the 7th position of Gut22 and a Val residue substituting for the Glu at the 10th position. The intrinsic fluorescence emission spectra indicated that the binding of Gut22 with lipid bilayer was much stronger than that of Gut22Ana. The leakage experiments with calcein-loaded liposomes showed that Gut22 strongly perturbed lipid bilayers while Gut22Ana did not. The apparent partition constant of Gut22 for partitioning into phosphatidylserine/phosphatidylcholine bilayers was measured; the effect of membrane potential on the interaction of Gut22 with lipid bilayers was studied and the conformation changes of Gut22 and Gut22Ana upon interacting with liposomes were studied by the method of circular dichroism analysis.
Wang
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Q
State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry, Chinese Academy of Sciences, China.
Cui
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D
Lin
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Q
D000595:Amino Acid Sequence; D004926:Escherichia coli; D008051:Lipid Bilayers; D008969:Molecular Sequence Data; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry; D021382:Protein Sorting Signals / Q000737:chemistry
D008051:Lipid Bilayers; D021382:Protein Sorting Signals; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C058558:phosphoenolpyruvate glucitol phosphotransferase