Interaction of arginine oligomer with model membrane
Abstract
Short oligomers of arginine (R8) have been shown to cross readily a variety of biological barriers. A hypothesis was put forward that inverted micelles form in biological membranes in the presence of arginine oligomer peptides, facilitating their transfer through the membranes. In order to define the role of peptide-lipid interaction in this mechanism, we prepared liposomes as the model membrane to study the ability of R8 inducing calcein release from liposomes, the fusion of liposomes, R8 binding to liposomes and membrane disturbing activity of the bound R8. The results show that R8 binding to liposome membrane depends on lipid compositions, negative surface charge density and interior water phase pH values of liposomes. R8 has no activity to induce the leakage of calcein from liposomes or improve liposome fusion. R8 does not permeabilize through the membrane spontaneously. These peptides delivering drugs through membranes may depend on receptors and energy.
- Authors:
-
- Department of Pharmacy, Tongji Medical College, Huazhong University of Science and Technology, No.13, Hangkong Road, Wuhan 430040 (China)
- National Laboratory of Biomacromolecules, Institute of Biophysics, The Chinese Academy of Science, Beijing 100101 (China)
- Publication Date:
- OSTI Identifier:
- 20991486
- Resource Type:
- Journal Article
- Journal Name:
- Biochemical and Biophysical Research Communications
- Additional Journal Information:
- Journal Volume: 359; Journal Issue: 4; Other Information: DOI: 10.1016/j.bbrc.2007.06.015; PII: S0006-291X(07)01232-6; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 60 APPLIED LIFE SCIENCES; ARGININE; CELL MEMBRANES; CHARGE DENSITY; CONFIGURATION MIXING; DRUGS; LIPIDS; LIPOSOMES; PEPTIDES; PH VALUE; RECEPTORS
Citation Formats
Yi, Dandan, Guoming, Li, Gao, Li, and Wei, Liang. Interaction of arginine oligomer with model membrane. United States: N. p., 2007.
Web. doi:10.1016/j.bbrc.2007.06.015.
Yi, Dandan, Guoming, Li, Gao, Li, & Wei, Liang. Interaction of arginine oligomer with model membrane. United States. https://doi.org/10.1016/j.bbrc.2007.06.015
Yi, Dandan, Guoming, Li, Gao, Li, and Wei, Liang. 2007.
"Interaction of arginine oligomer with model membrane". United States. https://doi.org/10.1016/j.bbrc.2007.06.015.
@article{osti_20991486,
title = {Interaction of arginine oligomer with model membrane},
author = {Yi, Dandan and Guoming, Li and Gao, Li and Wei, Liang},
abstractNote = {Short oligomers of arginine (R8) have been shown to cross readily a variety of biological barriers. A hypothesis was put forward that inverted micelles form in biological membranes in the presence of arginine oligomer peptides, facilitating their transfer through the membranes. In order to define the role of peptide-lipid interaction in this mechanism, we prepared liposomes as the model membrane to study the ability of R8 inducing calcein release from liposomes, the fusion of liposomes, R8 binding to liposomes and membrane disturbing activity of the bound R8. The results show that R8 binding to liposome membrane depends on lipid compositions, negative surface charge density and interior water phase pH values of liposomes. R8 has no activity to induce the leakage of calcein from liposomes or improve liposome fusion. R8 does not permeabilize through the membrane spontaneously. These peptides delivering drugs through membranes may depend on receptors and energy.},
doi = {10.1016/j.bbrc.2007.06.015},
url = {https://www.osti.gov/biblio/20991486},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 4,
volume = 359,
place = {United States},
year = {Fri Aug 10 00:00:00 EDT 2007},
month = {Fri Aug 10 00:00:00 EDT 2007}
}