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

0524535 - ÚOCHB 2021 RIV CH eng J - Článek v odborném periodiku
Pazderková, Markéta - Profant, V. - Maloň, P. - Dukor, R. K. - Čeřovský, Václav - Baumruk, V. - Bednárová, Lucie
Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges.
Symmetry-Basel. Roč. 12, č. 5 (2020), č. článku 812. E-ISSN 2073-8994
Grant CEP: GA ČR GAP208/10/0376; GA ČR GAP205/10/1276
Institucionální podpora: RVO:61388963
Klíčová slova: antimicrobial peptides * lasiocepsin * electronic circular dichroism * vibrational circular dichroism * Raman optical activity * disulfide group
Obor OECD: Biophysics
Impakt faktor: 2.713, rok: 2020
Způsob publikování: Open access
https://www.mdpi.com/2073-8994/12/5/812

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.
Trvalý link: http://hdl.handle.net/11104/0308881