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Computational Investigations of Arginine-Rich Peptides Interacting with Lipid Membranes.
- Source :
-
Macromolecular Theory & Simulations . Jul2015, Vol. 24 Issue 4, p399-406. 8p. - Publication Year :
- 2015
-
Abstract
- The translocation of hexa-arginine peptides across the asymmetric lipid bilayer in both random and bundled state was studied by coarse-grained molecular dynamics simulations. It was found that the peptides pass through the membrane by a pore-mediated mechanism when their concentration exceeds a critical value. However, the translocation efficiency of the bundled peptides is much higher than that of the random case at the same concentration. The pore formation results from the cumulative effects of each peptide in random case, while the bundled ones disturb the membrane locally. Furthermore, we show that the role of the hydrophobic group of peptide amphiphiles is facilitating the formation of aggregation for improving their penetration efficiency. [ABSTRACT FROM AUTHOR]
- Subjects :
- *ARGININE
*PEPTIDES
*MOLECULAR dynamics
*AMPHIPHILES
*DRUG delivery systems
Subjects
Details
- Language :
- English
- ISSN :
- 10221344
- Volume :
- 24
- Issue :
- 4
- Database :
- Academic Search Index
- Journal :
- Macromolecular Theory & Simulations
- Publication Type :
- Academic Journal
- Accession number :
- 108427364
- Full Text :
- https://doi.org/10.1002/mats.201500023