ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL
PEPTIDES

a 2020

ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL PEPTIDES

TÜRKOVÁ, Alžběta, Ivo KABELKA, Lukáš SUKENÍK, Šárka POKORNÁ, Martin Peter HOF et. al.

Basic information

Original name

ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL PEPTIDES

Authors

TÜRKOVÁ, Alžběta (203 Czech Republic, belonging to the institution), Ivo KABELKA (203 Czech Republic, belonging to the institution), Lukáš SUKENÍK (203 Czech Republic, belonging to the institution), Šárka POKORNÁ, Martin Peter HOF (276 Germany, belonging to the institution) and Robert VÁCHA (203 Czech Republic, belonging to the institution)

Edition

XXth INTERDISCIPLINARY MEETING OF YOUNG RESEARCHERS AND STUDENTS IN THE FIELD OF CHEMISTRY, BIOCHEMISTRY, MOLECULAR BIOLOGY, AND BIOMATERIALS, 2020

Other information

Language

English

Type of outcome

Konferenční abstrakt

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Czech Republic

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

RIV identification code

RIV/00216224:14740/20:00118418

Organization unit

Central European Institute of Technology

ISSN

Keywords in English

PROLINE/GLYCINE KINK

Abstract

V originále

Antimicrobial peptides (AMPs) can selectively disrupt bacterial membranes by the formation of leaky pores (see Fig. 1). Their selectivity and potency make them an appealing subject for drug development. Unfortunately, matching the peptide properties with their activity remains elusive. For instance, the role of proline/glycine kink in alfa-helical peptides was reported to both enhance and reduce the antimicrobial activity. In this work, we combined molecular dynamics simulations and fluorescence leakage assays to demonstrate that a helical kink stabilizes toroidal pores but disrupts barrel-stave pores. In addition, the exact position of the proline/glycine kink in the peptide sequence further controls the structure of toroidal pores. The provided molecular-level insight could be utilized for the design and modification of pore-forming antibacterial peptides.

Links

LQ1601, research and development project

Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

TÜRKOVÁ, Alžběta, Ivo KABELKA, Lukáš SUKENÍK, Šárka POKORNÁ, Martin Peter HOF and Robert VÁCHA. ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL PEPTIDES. In XXth INTERDISCIPLINARY MEETING OF YOUNG RESEARCHERS AND STUDENTS IN THE FIELD OF CHEMISTRY, BIOCHEMISTRY, MOLECULAR BIOLOGY, AND BIOMATERIALS. 2020. ISSN 2336-7202.

@proceedings{1753497,
   author = {Türková, Alžběta and Kabelka, Ivo and Sukeník, Lukáš and Pokorná, Šárka and Hof, Martin Peter and Vácha, Robert},
   booktitle = {XXth INTERDISCIPLINARY MEETING OF YOUNG RESEARCHERS AND STUDENTS IN THE FIELD OF CHEMISTRY, BIOCHEMISTRY, MOLECULAR BIOLOGY, AND BIOMATERIALS},
   keywords = {PROLINE/GLYCINE KINK},
   language = {eng},
   title = {ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL PEPTIDES},
   url = {http://www.interdisciplinarymeeting.cz/},
   year = {2020}
}

TY  - CONF
ID  - 1753497
AU  - Türková, Alžběta - Kabelka, Ivo - Sukeník, Lukáš - Pokorná, Šárka - Hof, Martin Peter - Vácha, Robert
PY  - 2020
TI  - ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL PEPTIDES
KW  - PROLINE/GLYCINE KINK
UR  - http://www.interdisciplinarymeeting.cz/
N2  - Antimicrobial peptides (AMPs) can selectively disrupt bacterial membranes by the formation of leaky pores (see Fig. 1). Their selectivity and potency make them an appealing subject for drug development. Unfortunately, matching the peptide properties with their activity remains elusive. For instance, the role of proline/glycine kink in alfa-helical peptides was reported to both enhance and reduce the antimicrobial activity. In this work, we combined molecular dynamics simulations and fluorescence leakage assays to demonstrate that a helical kink stabilizes toroidal pores but disrupts barrel-stave pores. In addition, the exact position of the proline/glycine kink in the peptide sequence further controls the structure of toroidal pores. The provided molecular-level insight could be utilized for the design and modification of pore-forming antibacterial peptides.
ER  -

TÜRKOVÁ, Alžběta, Ivo KABELKA, Lukáš SUKENÍK, Šárka POKORNÁ, Martin Peter HOF and Robert VÁCHA. ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL PEPTIDES. In \textit{XXth INTERDISCIPLINARY MEETING OF YOUNG RESEARCHERS AND STUDENTS IN THE FIELD OF CHEMISTRY, BIOCHEMISTRY, MOLECULAR BIOLOGY, AND BIOMATERIALS}. 2020. ISSN~2336-7202.

Detailed Information on Publication Record