Aggregation of Cateslytin β-Sheets on Negatively Charged Lipids Promotes Rigid Membrane Domains. A New Mode of Action for Antimicrobial Peptides?

Autor: Bernard Desbat, Frantz Jean-Francois, Marie-Hélène Metz-Boutigue, Benoit Odaert, Michel Roux, Sabine Castano, Erick J. Dufourc

Publikováno v: Biochemistry
Biochemistry, 2008, 47 (24), pp.6394-6402. ⟨10.1021/bi800448h⟩
Biochemistry, American Chemical Society, 2008, 47 (24), pp.6394-6402. ⟨10.1021/bi800448h⟩

Cateslytin, a positively charged (5+) arginine-rich antimicrobial peptide (bCgA, RSMRLSFRARGYGFR), was chemically synthesized and studied against membranes that mimic bacterial or mammalian systems. Circular dichroism, polarized attenuated total refl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc41ba2e568852000c183be921cdb45d
https://doi.org/10.1021/bi800448h

Membrane Interacting Peptides: From Killers to Helpers

Autor: Juan Elezgaray, Jeannot Toupe, Axelle Grélard, Cecile Loudet-Courreges, Marc-Antoine Sani, Lucie Khemtémourian, Erick J. Dufourc, Sébastien Buchoux, Benoit Odaert, Bernard Desbat, Frantz Jean-Francois, Michel Laguerre

Publikováno v: Current Protein and Peptide Science
Current Protein and Peptide Science, Bentham Science Publishers, 2012, 13 (7), pp.620-631. ⟨10.2174/138920312804142138⟩
Current protein & peptide science
Current protein & peptide science, 2012, 13 (7), pp.620-631. ⟨10.2174/138920312804142138⟩
Current Protein and Peptide Science, 2012, 13 (7), pp.620-631. ⟨10.2174/138920312804142138⟩

International audience; Membrane interacting peptides are reviewed in terms of structure and mode of action on lipid membranes. Helical, β-stranded, peptides containing both helices and strands, cyclic, lipopeptides and short linear peptides are see

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb4030ddea86e534c25db390d405457c
https://hal.archives-ouvertes.fr/hal-00748185

Disordered Pore Formation At Rigid/Fluid Boundary Zones As A New Mechanism For Peptide-Membrane Interaction With The Beta-sheeted Antimicrobial Peptide Cateslytin

Autor: Erick J. Dufourc, Juan Elezgaray, Frantz Jean-Francois, Marie-Héléine Metz-Boutigue

Publikováno v: Biophysical Journal
Biophysical Journal, Biophysical Society, 2009, 96 (3), pp.390a. ⟨10.1016/j.bpj.2008.12.2911⟩

The peptide cateslytin (RSMRLSFRARGYGFR) produced by enzymatic degradation of stress proteins is remarkably active against a large number of microorganisms including Plasmodium Falciparum responsible for Malaria. Its mode of action on membranes mimic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bb51054248e142e46ac7b8082533a4e
https://hal.archives-ouvertes.fr/hal-02124169

Variability in secondary structure of the antimicrobial peptide Cateslytin in powder, solution, DPC micelles and at the air-water interface

Autor: Claude Manigand, Marie-Hélène Metz-Boutigue, Frantz Jean-Francois, Katell Bathany, Benoit Odaert, Axelle Grélard, Sabine Castano, Erick J. Dufourc, Lucie Khemtémourian

Publikováno v: European Biophysics Journal
European Biophysics Journal, 2007, 36 ((8)), pp.1019-27. ⟨10.1007/s00249-007-0169-8⟩
European Biophysics Journal, Springer Verlag (Germany), 2007, 36 ((8)), pp.1019-27. ⟨10.1007/s00249-007-0169-8⟩

International audience; Cateslytin (bCGA (344)RSMRLSFRARGYGFR(358)), a five positively charged 15 amino-acid residues arginine-rich antimicrobial peptide, was synthesized using a very efficient procedure leading to high yields and to a 99% purity as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14eb5d822fe4b84e7eebc99db9e965b8
https://hal.science/hal-00689903

Heterooligomerization of Membrane Peptides Involved in Tuberculosis: MgtC and MgtR

Autor: Frantz Jean-Francois, Alissa Myrick, Likai Song, Eric J. Rubin, Timothy A. Cross

Publikováno v: Biophysical Journal. (3):422a

Recent results have converged to highlight the role of hydrophobic peptides that form a novel class of active molecules in Escherichia coli and Salmonella enterica serovar Typhimurium. These peptides are apparently able to interact with membrane prot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92afee98cba16046a913292c1401c3d9