The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition.

Ros, Uris

The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition. [electronic resource] - Journal of biosciences Dec 2011 - 781-91 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

0973-7138

10.1007/s12038-011-9156-4 doi


Amino Acid Sequence
Cnidarian Venoms--chemical synthesis
Hydrophobic and Hydrophilic Interactions
Lipid Bilayers--chemistry
Membrane Lipids--chemistry
Molecular Sequence Data
Organic Chemicals--chemical synthesis
Peptide Fragments--chemical synthesis
Permeability
Protein Binding
Unilamellar Liposomes--chemistry