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De Cuyper M, Bulte JW. Preparation and Characterization of a Phospholipid Membrane-Bound Tetrapeptide That Corresponds to the C-Terminus of the Gastrin/Cholecystokinin Hormone Family. J Colloid Interface Sci. 2000;227(2):421-426doi: 10.1006/jcis.2000.6902.
De Cuyper M, & Bulte, J. W. (2000). Preparation and Characterization of a Phospholipid Membrane-Bound Tetrapeptide That Corresponds to the C-Terminus of the Gastrin/Cholecystokinin Hormone Family. Journal of colloid and interface science, 227(2), 421-426. https://doi.org/10.1006/jcis.2000.6902
De Cuyper M, and Bulte. "Preparation and Characterization of a Phospholipid Membrane-Bound Tetrapeptide That Corresponds to the C-Terminus of the Gastrin/Cholecystokinin Hormone Family." Journal of colloid and interface science vol. 227,2 (2000): 421-426. doi: https://doi.org/10.1006/jcis.2000.6902
De Cuyper M, Bulte JW. Preparation and Characterization of a Phospholipid Membrane-Bound Tetrapeptide That Corresponds to the C-Terminus of the Gastrin/Cholecystokinin Hormone Family. J Colloid Interface Sci. 2000 Jul 15;227(2):421-426. doi: 10.1006/jcis.2000.6902. PMID: 10873329.
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J Colloid Interface Sci. 2000 Jul 15;227(2):421-426. doi: 10.1006/jcis.2000.6902.

Preparation and Characterization of a Phospholipid Membrane-Bound Tetrapeptide That Corresponds to the C-Terminus of the Gastrin/Cholecystokinin Hormone Family.

Journal of colloid and interface science

De Cuyper M, Bulte

Affiliations

  1. Interdisciplinary Research Centre, Katholieke Universiteit Leuven-Campus Kortrijk, Kortrijk, B-8500, Belgium

PMID: 10873329 DOI: 10.1006/jcis.2000.6902

Abstract

The present work deals with the synthesis of a hydrophobized peptide and its localization at the membrane surface, after its incorporation into phospholipid vesicles. The tetrapeptide, Trp-Met-Asp-Phe-NH(2), which corresponds to the C-terminus of the cholecystokinin/gastrin hormone family, is conjugated to N-glutaryldioleoylphosphatidylethanolamine using a carbodiimide-catalyzed reaction method. Sonication of the lipophilized hormone in the presence of dimyristoylphosphatidylcholine results in a strong sequestration of the conjugate in the artificial membrane structures that are formed. More detailed information on the localization of the peptide moiety with respect to the membrane surface is gathered from fluorescence measurements. Both the observed blue shift in the fluorescence spectra and the quenching of Trp emission in the presence of potassium iodide point to a partial screening of the hormone moiety from the surrounding aqueous phase. The different parameters that may influence the physicochemical behavior of a hydrophobized peptide in a membrane structure are briefly discussed Copyright 2000 Academic Press.

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