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Effect of Helical Kink on Peptide Translocation across Phospholipid Membranes

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00114328" target="_blank" >RIV/00216224:14740/20:00114328 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1021/acs.jpcb.0c03291" target="_blank" >https://doi.org/10.1021/acs.jpcb.0c03291</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acs.jpcb.0c03291" target="_blank" >10.1021/acs.jpcb.0c03291</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Effect of Helical Kink on Peptide Translocation across Phospholipid Membranes

  • Original language description

    Biological membranes present a major obstacle for the delivery of therapeutic agents into cells. Some peptides have been shown to translocate across the membrane spontaneously, and they could be thus used as drug-carriers. However, the advantageous peptide properties for the translocation remain unclear. Of particular interest is the effect of a proline-induced kink in alpha-helical peptides, because the kink was previously reported to both increase and decrease the antimicrobial activity. The antimicrobial activity of peptides could be related to their translocation across the membrane as is the case of the buforin 2 peptide investigated here. Using computer simulations with two independent models, we consistently showed that the presence of the kink has (1) no effect on the translocation barrier, (2) reduces the peptide affinity to the membrane, and (3) disfavors the transmembrane state. Moreover, we were able to determine that these effects are mainly caused by the peptide increased polarity, not the increased flexibility of the kink. The provided molecular understanding can be utilized for the design of cell-penetrating and drug-carrying peptides.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10403 - Physical chemistry

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    The Journal of Physical Chemistry B

  • ISSN

    1520-6106

  • e-ISSN

    1520-5207

  • Volume of the periodical

    124

  • Issue of the periodical within the volume

    28

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    8

  • Pages from-to

    5940-5947

  • UT code for WoS article

    000551541600017

  • EID of the result in the Scopus database

    2-s2.0-85087670337