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Open AccessFeature PaperArticle

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

1
Faculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 121 16 Prague 2, Czech Republic
2
Institute of Organic Chemistry and Biochemistry AS CR v.v.i., Fleming Square 2, 166 10 Prague 6, Czech Republic
3
BioTools, Inc., 17546 Bee Line Highway, Jupiter, FL 33548, USA
*
Authors to whom correspondence should be addressed.
Symmetry 2020, 12(5), 812; https://doi.org/10.3390/sym12050812
Received: 17 April 2020 / Revised: 1 May 2020 / Accepted: 7 May 2020 / Published: 13 May 2020
(This article belongs to the Special Issue Symmetric and Asymmetric Structure in Drug Design and Biomolecules)
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. View Full-Text
Keywords: antimicrobial peptides; lasiocepsin; electronic circular dichroism; vibrational circular dichroism; Raman optical activity; disulfide group antimicrobial peptides; lasiocepsin; electronic circular dichroism; vibrational circular dichroism; Raman optical activity; disulfide group
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MDPI and ACS Style

Pazderková, M.; Profant, V.; Maloň, P.; Dukor, R.K.; Čeřovský, V.; Baumruk, V.; Bednárová, L. Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges. Symmetry 2020, 12, 812. https://doi.org/10.3390/sym12050812

AMA Style

Pazderková M, Profant V, Maloň P, Dukor RK, Čeřovský V, Baumruk V, Bednárová L. Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges. Symmetry. 2020; 12(5):812. https://doi.org/10.3390/sym12050812

Chicago/Turabian Style

Pazderková, Markéta; Profant, Václav; Maloň, Petr; Dukor, Rina K.; Čeřovský, Václav; Baumruk, Vladimír; Bednárová, Lucie. 2020. "Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges" Symmetry 12, no. 5: 812. https://doi.org/10.3390/sym12050812

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