Design and synthesis of amphipathic 3(10)-helical peptides and their interactions with phospholipid bilayers and ion channel formation.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference29 articles.
1. Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic alpha-helical model peptides of various chain lengths.
2. Formation of ion channels in planar lipid bilayer membranes by synthetic basic peptides
3. Atomic co-ordinates for an α-helix: Refinement of the crystal structure of α-poly-l-alanine
4. Helix geometry in proteins
5. Determination of the helix and β form of proteins in aqueous solution by circular dichroism
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1. Systematic Design and Validation of Ion Channel Stabilization of Amphipathic α-Helical Peptides Incorporating Tryptophan Residues;ACS Omega;2020-12-29
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3. Utilizing Electron Spin Echo Envelope Modulation To Distinguish between the Local Secondary Structures of an α-Helix and an Amphipathic 310-Helical Peptide;The Journal of Physical Chemistry B;2017-03-31
4. Conformational Changes and Association of Membrane-Interacting Peptides in Myelin Membrane Models: A Case of the C-Terminal Peptide of Proteolipid Protein and the Antimicrobial Peptide Melittin;The Journal of Physical Chemistry B;2015-11-12
5. Formation of ion-selective channel using cyclic tetrapeptides;Bioorganic & Medicinal Chemistry;2012-01
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