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Lasiocepsin, a novel cyclic antimicrobial peptide from the venom of eusocial bee Lasioglossum laticeps (Hymenoptera: Halictidae)

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F12%3A00379681" target="_blank" >RIV/61388963:_____/12:00379681 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1007/s00726-011-1125-6" target="_blank" >http://dx.doi.org/10.1007/s00726-011-1125-6</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s00726-011-1125-6" target="_blank" >10.1007/s00726-011-1125-6</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Lasiocepsin, a novel cyclic antimicrobial peptide from the venom of eusocial bee Lasioglossum laticeps (Hymenoptera: Halictidae)

  • Original language description

    In the venom of eusocial bee Lasioglossum laticeps, we identified a novel unique antimicrobial peptide named lasiocepsin consisting of 27 amino acid residues and two disulfide bridges. After identifying its primary structure, we synthesized lasiocepsin by solid-phase peptide synthesis using two different approaches for oxidative folding. The oxidative folding of fully deprotected linear peptide resulted in a mixture of three products differing in the pattern of disulfide bridges. Regioselective disulfide bond formation significantly improved the yield of desired product. The synthetic lasiocepsin possessed antimicrobial activity against both Gram-positive and -negative bacteria, antifungal activity against Candida albicans, and no hemolytic activity against human erythrocytes. We synthesized two lasiocepsin analogs cyclized through one native disulfide bridge in different positions and having the remaining two cysteines substituted by alanines. The analog cyclized through a Cys8-Cys25

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

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

    2012

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Amino Acids

  • ISSN

    0939-4451

  • e-ISSN

  • Volume of the periodical

    43

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    AT - AUSTRIA

  • Number of pages

    11

  • Pages from-to

    751-761

  • UT code for WoS article

    000306365500023

  • EID of the result in the Scopus database