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Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F20%3A00524535" target="_blank" >RIV/61388963:_____/20:00524535 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11320/20:10422780

  • Result on the web

    <a href="https://www.mdpi.com/2073-8994/12/5/812" target="_blank" >https://www.mdpi.com/2073-8994/12/5/812</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/sym12050812" target="_blank" >10.3390/sym12050812</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges

  • Original language description

    We report an investigation of the role of disulfide bridges in the 27-residue antimicrobial peptide lasiocepsin (I) containing two disulfide groups (Cys8–Cys25, Cys17–Cys27) and three its analogs lacking one (II, III) or both (IV) native disulfides. Selective alternate incorporation of one or both disulfide bridges influences symmetry, conformation and biological properties of these peptides as demonstrated in their chiroptical (particularly Raman) properties. The effect of modifying the disulfide bridge pattern on the peptide secondary structure is investigated in water and in the presence of 2,2,2-trifluoroethanol and sodium dodecyl sulphate. A combination of experimental electronic and vibrational chiroptical data shows that both disulfide groups are necessary for stabilizing lasiocepsin secondary structure. While the Cys8–Cys25 disulfide group is important for sustaining lasiocepsin tertiary structure and maintaining its biological activity, the Cys17–Cys27 disulfide bridge has a supporting function consisting in reducing peptide flexibility.

  • 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

    10610 - Biophysics

Result continuities

  • Project

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

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

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

    Symmetry-Basel

  • ISSN

    2073-8994

  • e-ISSN

  • Volume of the periodical

    12

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    22

  • Pages from-to

    812

  • UT code for WoS article

    000540226400130

  • EID of the result in the Scopus database

    2-s2.0-85085642389