TÜRKOVÁ, Alžběta, Ivo KABELKA, Tereza KRÁLOVÁ, Lukáš SUKENÍK, S. POKORNÁ, M. HOF and Robert VÁCHA. Kink in Helical Peptides Affects Membrane Pore Formation. 2019. ISSN 0006-3495. Available from: https://dx.doi.org/10.1016/j.bpj.2018.11.2760.
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Basic information
Original name Kink in Helical Peptides Affects Membrane Pore Formation
Authors TÜRKOVÁ, Alžběta (203 Czech Republic, belonging to the institution), Ivo KABELKA (203 Czech Republic, belonging to the institution), Tereza KRÁLOVÁ (203 Czech Republic, belonging to the institution), Lukáš SUKENÍK (203 Czech Republic, belonging to the institution), S. POKORNÁ (203 Czech Republic), M. HOF and Robert VÁCHA (203 Czech Republic, guarantor, belonging to the institution).
Edition 2019.
Other information
Original language English
Type of outcome Conference abstract
Field of Study 10403 Physical chemistry
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW Kink in Helical Peptides Affects Membrane Pore Formation
Impact factor Impact factor: 3.854
RIV identification code RIV/00216224:14310/19:00112870
Organization unit Faculty of Science
ISSN 0006-3495
Doi http://dx.doi.org/10.1016/j.bpj.2018.11.2760
UT WoS 000460779802573
Keywords in English Kink; Helical Peptides
Tags rivok
Tags International impact
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 1/4/2020 15:51.
Abstract
Antimicrobial peptides (AMPs) can kill pathogenic cells via the formation of membrane pores. However, the connection between peptide properties and their effect on pore formation remains elusive. In particular, the role of proline/glycine kink in helical AMPs has been reported with contradictory effects on antimicrobial activity. Using computer simulations and fluorescence leakage experiments we show the relationship between alpha-helical kink and the structure of the formed pore. Reconciling previous data, the presence of kinks was found to have both stabilizing or destabilizing effect, depending on the pore structure. Moreover, the position of proline/glycine kink in AMP sequence controls the peptide arrangements in the stabilized pores. The provided knowledge can be utilized to rationally design peptides with different ability to form membrane pores useful for the development of new antibacterial agents. To read this article in full you will need to make a payment
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