Počet záznamů: 1
Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges
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SYSNO ASEP 0524535 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges Tvůrce(i) 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, ORCIDČíslo článku 812 Zdroj.dok. Symmetry-Basel. - : MDPI - ISSN 2073-8994
Roč. 12, č. 5 (2020)Poč.str. 22 s. Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova antimicrobial peptides ; lasiocepsin ; electronic circular dichroism ; vibrational circular dichroism ; Raman optical activity ; disulfide group Vědní obor RIV BO - Biofyzika Obor OECD Biophysics CEP GAP208/10/0376 GA ČR - Grantová agentura ČR GAP205/10/1276 GA ČR - Grantová agentura ČR Způsob publikování Open access Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000540226400130 EID SCOPUS 85085642389 DOI https://doi.org/10.3390/sym12050812 Anotace 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. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Rok sběru 2021 Elektronická adresa https://www.mdpi.com/2073-8994/12/5/812
Počet záznamů: 1