Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges
We report an investigation of the role of disulfide bridges in the 27-residue antimicrobial peptide lasiocepsin (<b>I</b>) containing two disulfide groups (Cys<sup>8</sup>–Cys<sup>25</sup>, Cys<sup>17</sup>–Cys<sup>27</sup>) and three its a...
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MDPI AG
2020-05-01
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| Series: | Symmetry |
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| Online Access: | https://www.mdpi.com/2073-8994/12/5/812 |
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| author | Markéta Pazderková Václav Profant Petr Maloň Rina K. Dukor Václav Čeřovský Vladimír Baumruk Lucie Bednárová |
| author_facet | Markéta Pazderková Václav Profant Petr Maloň Rina K. Dukor Václav Čeřovský Vladimír Baumruk Lucie Bednárová |
| author_sort | Markéta Pazderková |
| collection | DOAJ |
| description | We report an investigation of the role of disulfide bridges in the 27-residue antimicrobial peptide lasiocepsin (<b>I</b>) containing two disulfide groups (Cys<sup>8</sup>–Cys<sup>25</sup>, Cys<sup>17</sup>–Cys<sup>27</sup>) and three its analogs lacking one (<b>II</b>, <b>III</b>) or both (<b>IV</b>) 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 Cys<sup>8</sup>–Cys<sup>25</sup> disulfide group is important for sustaining lasiocepsin tertiary structure and maintaining its biological activity, the Cys<sup>17</sup>–Cys<sup>27</sup> disulfide bridge has a supporting function consisting in reducing peptide flexibility. |
| first_indexed | 2024-03-10T19:51:53Z |
| format | Article |
| id | doaj.art-c0c0a69468814713961e76eea17070ca |
| institution | Directory Open Access Journal |
| issn | 2073-8994 |
| language | English |
| last_indexed | 2024-03-10T19:51:53Z |
| publishDate | 2020-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Symmetry |
| spelling | doaj.art-c0c0a69468814713961e76eea17070ca2023-11-20T00:17:33ZengMDPI AGSymmetry2073-89942020-05-0112581210.3390/sym12050812Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide BridgesMarkéta Pazderková0Václav Profant1Petr Maloň2Rina K. Dukor3Václav Čeřovský4Vladimír Baumruk5Lucie Bednárová6Faculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 121 16 Prague 2, Czech RepublicFaculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 121 16 Prague 2, Czech RepublicFaculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 121 16 Prague 2, Czech RepublicBioTools, Inc., 17546 Bee Line Highway, Jupiter, FL 33548, USAInstitute of Organic Chemistry and Biochemistry AS CR v.v.i., Fleming Square 2, 166 10 Prague 6, Czech RepublicFaculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 121 16 Prague 2, Czech RepublicInstitute of Organic Chemistry and Biochemistry AS CR v.v.i., Fleming Square 2, 166 10 Prague 6, Czech RepublicWe report an investigation of the role of disulfide bridges in the 27-residue antimicrobial peptide lasiocepsin (<b>I</b>) containing two disulfide groups (Cys<sup>8</sup>–Cys<sup>25</sup>, Cys<sup>17</sup>–Cys<sup>27</sup>) and three its analogs lacking one (<b>II</b>, <b>III</b>) or both (<b>IV</b>) 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 Cys<sup>8</sup>–Cys<sup>25</sup> disulfide group is important for sustaining lasiocepsin tertiary structure and maintaining its biological activity, the Cys<sup>17</sup>–Cys<sup>27</sup> disulfide bridge has a supporting function consisting in reducing peptide flexibility.https://www.mdpi.com/2073-8994/12/5/812antimicrobial peptideslasiocepsinelectronic circular dichroismvibrational circular dichroismRaman optical activitydisulfide group |
| spellingShingle | Markéta Pazderková Václav Profant Petr Maloň Rina K. Dukor Václav Čeřovský Vladimír Baumruk Lucie Bednárová Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges Symmetry antimicrobial peptides lasiocepsin electronic circular dichroism vibrational circular dichroism Raman optical activity disulfide group |
| title | Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges |
| title_full | Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges |
| title_fullStr | Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges |
| title_full_unstemmed | Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges |
| title_short | Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges |
| title_sort | chiroptical properties and conformation of four lasiocepsin related antimicrobial peptides structural role of disulfide bridges |
| topic | antimicrobial peptides lasiocepsin electronic circular dichroism vibrational circular dichroism Raman optical activity disulfide group |
| url | https://www.mdpi.com/2073-8994/12/5/812 |
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