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

SYSNO ASEP	0524535
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges
Author(s)	Pazderková, Markéta (UOCHB-X)_{RID, ORCID} Profant, V. (CZ) Maloň, P. (CZ) Dukor, R. K. (US) Čeřovský, Václav (UOCHB-X)_{RID, ORCID} Baumruk, V. (CZ) Bednárová, Lucie (UOCHB-X)_{RID, ORCID}
Article number	812
Source Title	Symmetry-Basel. - : MDPI Roč. 12, č. 5 (2020)
Number of pages	22 s.
Language	eng - English
Country	CH - Switzerland
Keywords	antimicrobial peptides ; lasiocepsin ; electronic circular dichroism ; vibrational circular dichroism ; Raman optical activity ; disulfide group
Subject RIV	BO - Biophysics
OECD category	Biophysics
R&D Projects	GAP208/10/0376 GA ČR - Czech Science Foundation (CSF)
	GAP205/10/1276 GA ČR - Czech Science Foundation (CSF)
Method of publishing	Open access
Institutional support	UOCHB-X - RVO:61388963
UT WOS	000540226400130
EID SCOPUS	85085642389
DOI	10.3390/sym12050812
Annotation	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.
Workplace	Institute of Organic Chemistry and Biochemistry
Contact	asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434
Year of Publishing	2021
Electronic address	https://www.mdpi.com/2073-8994/12/5/812

Number of the records: 1