In situ captured antibacterial action of membrane-incising
peptide lamellae

J 2024

In situ captured antibacterial action of membrane-incising peptide lamellae

KAMAL, el Battioui; Sohini CHAKRABORTY; Andras WACHA; Daniel MOLNAR; Mayra QUEME-PENA et. al.

Základní údaje

Originální název

In situ captured antibacterial action of membrane-incising peptide lamellae

Autoři

Vydání

Nature Communications, Berlin, Nature, 2024, 2041-1723

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10400 1.4 Chemical sciences

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 15.700

Kód RIV

RIV/00216224:90127/24:00139987

Organizační jednotka

CIISB II

DOI

https://doi.org/10.1038/s41467-024-47708-4

UT WoS

001207290500005

EID Scopus

2-s2.0-85191042046

Klíčová slova anglicky

HELICAL SECONDARY STRUCTURE; BETA-PEPTIDE; ANTIMICROBIAL PEPTIDES; CONFORMATIONAL CONVERSION; MOLECULAR-DYNAMICS; AMINO-ACIDS; FOLDAMERS; MECHANISM; BINDING; PROTEIN

Štítky

CF CRYO, ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 7. 5. 2025 12:54, Mgr. Eva Dubská

Anotace

V originále

Developing unique mechanisms of action are essential to combat the growing issue of antimicrobial resistance. Supramolecular assemblies combining the improved biostability of non-natural compounds with the complex membrane-attacking mechanisms of natural peptides are promising alternatives to conventional antibiotics. However, for such compounds the direct visual insight on antibacterial action is still lacking. Here we employ a design strategy focusing on an inducible assembly mechanism and utilized electron microscopy (EM) to follow the formation of supramolecular structures of lysine-rich heterochiral beta 3-peptides, termed lamellin-2K and lamellin-3K, triggered by bacterial cell surface lipopolysaccharides. Combined molecular dynamics simulations, EM and bacterial assays confirmed that the phosphate-induced conformational change on these lamellins led to the formation of striped lamellae capable of incising the cell envelope of Gram-negative bacteria thereby exerting antibacterial activity. Our findings also provide a mechanistic link for membrane-targeting agents depicting the antibiotic mechanism derived from the in-situ formation of active supramolecules.

Návaznosti

90242, velká výzkumná infrastruktura

Název: CIISB III

Citovat

KAMAL, el Battioui; Sohini CHAKRABORTY; Andras WACHA; Daniel MOLNAR; Mayra QUEME-PENA; Imola Cs SZIGYARTO; Csenge Lilla SZABO; Andrea BODOR; Kata HORVATI; Gergo GYULAI; Szilvia BOSZE; Judith MIHALY; Balint JEZSO; Lorand ROMANSZKI; Judit TOTH; Zoltan VARGA; Istvan MANDITY; Tuende JUHASZ a Tamas BEKE-SOMFAI. In situ captured antibacterial action of membrane-incising peptide lamellae. Nature Communications. Berlin: Nature, 2024, roč. 15, č. 1, s. 1-14. ISSN 2041-1723. Dostupné z: https://doi.org/10.1038/s41467-024-47708-4.

@article{2484241,
   author = {Kamal, el Battioui and Chakraborty, Sohini and Wacha, Andras and Molnar, Daniel and QuemeandPena, Mayra and Szigyarto, Imola Cs and Szabo, Csenge Lilla and Bodor, Andrea and Horvati, Kata and Gyulai, Gergo and Bosze, Szilvia and Mihaly, Judith and Jezso, Balint and Romanszki, Lorand and Toth, Judit and Varga, Zoltan and Mandity, Istvan and Juhasz, Tuende and BekeandSomfai, Tamas},
   article_location = {Berlin},
   article_number = {1},
   doi = {https://doi.org/10.1038/s41467-024-47708-4},
   keywords = {HELICAL SECONDARY STRUCTURE; BETA-PEPTIDE; ANTIMICROBIAL PEPTIDES; CONFORMATIONAL CONVERSION; MOLECULAR-DYNAMICS; AMINO-ACIDS; FOLDAMERS; MECHANISM; BINDING; PROTEIN},
   language = {eng},
   issn = {2041-1723},
   journal = {Nature Communications},
   title = {In situ captured antibacterial action of membrane-incising peptide lamellae},
   url = {https://www.nature.com/articles/s41467-024-47708-4},
   volume = {15},
   year = {2024}
}

TY  - JOUR
ID  - 2484241
AU  - Kamal, el Battioui - Chakraborty, Sohini - Wacha, Andras - Molnar, Daniel - Queme-Pena, Mayra - Szigyarto, Imola Cs - Szabo, Csenge Lilla - Bodor, Andrea - Horvati, Kata - Gyulai, Gergo - Bosze, Szilvia - Mihaly, Judith - Jezso, Balint - Romanszki, Lorand - Toth, Judit - Varga, Zoltan - Mandity, Istvan - Juhasz, Tuende - Beke-Somfai, Tamas
PY  - 2024
TI  - In situ captured antibacterial action of membrane-incising peptide lamellae
JF  - Nature Communications
VL  - 15
IS  - 1
SP  - 1-14
EP  - 1-14
PB  - Nature
SN  - 20411723
KW  - HELICAL SECONDARY STRUCTURE
KW  - BETA-PEPTIDE
KW  - ANTIMICROBIAL PEPTIDES
KW  - CONFORMATIONAL CONVERSION
KW  - MOLECULAR-DYNAMICS
KW  - AMINO-ACIDS
KW  - FOLDAMERS
KW  - MECHANISM
KW  - BINDING
KW  - PROTEIN
UR  - https://www.nature.com/articles/s41467-024-47708-4
N2  - Developing unique mechanisms of action are essential to combat the growing issue of antimicrobial resistance. Supramolecular assemblies combining the improved biostability of non-natural compounds with the complex membrane-attacking mechanisms of natural peptides are promising alternatives to conventional antibiotics. However, for such compounds the direct visual insight on antibacterial action is still lacking. Here we employ a design strategy focusing on an inducible assembly mechanism and utilized electron microscopy (EM) to follow the formation of supramolecular structures of lysine-rich heterochiral beta 3-peptides, termed lamellin-2K and lamellin-3K, triggered by bacterial cell surface lipopolysaccharides. Combined molecular dynamics simulations, EM and bacterial assays confirmed that the phosphate-induced conformational change on these lamellins led to the formation of striped lamellae capable of incising the cell envelope of Gram-negative bacteria thereby exerting antibacterial activity. Our findings also provide a mechanistic link for membrane-targeting agents depicting the antibiotic mechanism derived from the in-situ formation of active supramolecules.
ER  -

KAMAL, el Battioui; Sohini CHAKRABORTY; Andras WACHA; Daniel MOLNAR; Mayra QUEME-PENA; Imola Cs SZIGYARTO; Csenge Lilla SZABO; Andrea BODOR; Kata HORVATI; Gergo GYULAI; Szilvia BOSZE; Judith MIHALY; Balint JEZSO; Lorand ROMANSZKI; Judit TOTH; Zoltan VARGA; Istvan MANDITY; Tuende JUHASZ a Tamas BEKE-SOMFAI. In situ captured antibacterial action of membrane-incising peptide lamellae. \textit{Nature Communications}. Berlin: Nature, 2024, roč.~15, č.~1, s.~1-14. ISSN~2041-1723. Dostupné z: https://doi.org/10.1038/s41467-024-47708-4.

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