Perturbation of the lipid bilayer of model membranes by synthetic signal peptides

Nagaraj, Ramakrishnan ; Joseph, Mercy ; Reddy, Gundlapally Laxma (1987) Perturbation of the lipid bilayer of model membranes by synthetic signal peptides Biochimica et Biophysica Acta: Biomembranes, 903 (3). pp. 465-472. ISSN 0005-2736

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The interaction of synthetic peptides corresponding to the signal sequences of Escherichia coli alkaline phosphatase: Lys-Gln-Ser-Thr-Ile-Ala-Leu-Ala-Leu-Leu-Pro-Leu-Leu-Phe-Thr-Pro-Val-Thr-Lys-Ala-OCH3, chicken lysozyme: Met-Lys-Ser-Leu-Leu-Ile-Leu-Val-Leu-Cys(Bzl)-Phe-Leu-Pro-Leu-Ala-Ala-Leu-Gly-OCH2-C6H5 and variant of the chicken lysozyme signal sequence with a charged residue in the hydrophobic region: Lys-Leu-Leu-Ile-Ala-Leu-Val-Leu-Lys-Phe-Leu-Pro-Leu-Ala-Ala-Leu-Gly-OCH3 with model membranes of brain phosphatidylserine (PS) and egg phosphatidylcholine (PC) have been investigated by 90° light scattering and fluorescence spectroscopy. Our results indicate that the association of signal peptides with model membranes results in extensive perturbation of the lipid bilayer so as to cause fusion of PS vesicles and aggregation of PC vesicles. The vesicles are also rendered permeable to hydrophilic molecules like carboxyfluorescein. The variant peptide with the lysine residue in the hydrophobic region also has the ability to perturb lipid bilayers of model membranes.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Lipid Bilayer; Fluorescence; Model Membrane; Synthetic Signal Peptide; Signal Peptide
ID Code:24029
Deposited On:01 Dec 2010 12:43
Last Modified:01 Dec 2010 12:43

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