Membrane pore-formation correlates with the hydrophilic angle of histidine-rich amphipathic peptides with multiple biological activities-Reference-Cited by-同舟云学术

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Membrane pore-formation correlates with the hydrophilic angle of histidine-rich amphipathic peptides with multiple biological activities

Published:2020-08 Issue:8 Volume:1862 Page:183212
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Lointier Morane,Aisenbrey Christopher,Marquette Arnaud,Tan Jia Hao,Kichler Antoine,Bechinger Burkhard

Funder

Agence Nationale de la Recherche

University of Strasbourg

CNRS

Région Alsace

RTRA International Center of Frontier Research in Chemistry

FRM

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference34 articles.

1. Towards membrane protein design: pH-sensitive topology of histidine-containing polypeptides;Bechinger;J. Mol. Biol.,1996

2. NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action and DNA transfection;Georgescu;Biophys. J.,2010

3. The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers: the effects of charges and pH;Vogt;J. Biol. Chem.,1999

4. Interactions involved in the realignment of membrane-associated helices: an investigation using oriented solid-state NMR and ATR-FTIR spectroscopies topologies;Aisenbrey;J. Biol. Chem.,2006

5. Translocation of amino acyl residues from the membrane interface to the hydrophobic core: thermodynamic model and experimental analysis using ATR-FTIR spectroscopy;Aisenbrey;Mol. Membr. Biol.,2006

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