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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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