Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges
Abstract
:1. Introduction
2. Materials and Methods
3. Results
3.1. Secondary Structuture Assignement of I–IV in Water
3.1.1. Electronic Circular Dichroism
3.1.2. Vibrational Spectroscopy
3.2. Structural Changes of I–IV due to the Presence of TFE and SDS
3.2.1. Structural Changes Followed by ECD
3.2.2. Structural Changes Followed by Vibrational Spectroscopy
3.3. Summarization of the Results
- Secondary structure of I in water, as derived from ECD, IR/VCD, and Raman/ROA data, corresponds well to the published NMR structure.
- The native peptide I manifests high structural and conformational rigidity, as evidenced by ROA data. While the analog II appears to be still conformationally rigid (although to somewhat lesser extent than I), the analogs III and IV seem to be rather flexible. The analog IV is the most flexible one.
- In the presence of TFE (>20%) or SDS (>2 mM), all the analogs form α-helical structure (at least to some extent) with some random coil/PPII structure participation. On the contrary, in H2O the α-helical structure is observed only for the natural peptide I.
- Based on the ROA spectra, hydrated form of α-helical structure seems to prevail in all the analogs I–IV in the presence of SDS. Analogs II and IV seem to also have a considerable portion of unhydrated α-helical structure.
- According to the Raman spectra, the disulfide groups of I–III in water adopt predominantly the gauche-gauche-gauche conformation. In the presence of SDS, gauche-gauche-gauche conformation remains dominant in I and III, while for II we observe a conformational change to gauche-gauche-trans and trans-gauche-trans conformation.
- Both ECD and ROA spectra indicate structural changes in absolute configuration of disulfide groups upon addition of SDS.
4. Discussion
5. Conclusions
Supplementary Materials
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
References
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ILasiocepsin Analogs | Antimicrobial Activity MIC (μM) | |||||
---|---|---|---|---|---|---|
(mg/mL) | ||||||
B.s. | S.a. | E.c. | P.a. | C.a. | ||
I | GLPRKILCAIAKKKGKCKGPLKLVCKC | 0.4 | 93 | 8.6 | 15 | 3.6 |
0.001 | 0.269 | 0.025 | 0.04 | 0.01 | ||
II | GLPRKILAAIAKKKGKCKGPLKLVAKC | 4.2 | >100 | >100 | >100 | 50 |
0.012 | >0.283 | >0.283 | >0.283 | 0.0141 | ||
III | GLPRKILCAIAKKKGKAKGPLKLVCKA | 0.5 | >100 | 55 | 65 | 70 |
0.001 | >0.283 | 0.156 | 0.184 | 0.0198 | ||
IV | GLPRKILAAIAKKKGKAKGPLKLVAKA | 12 | >100 | >100 | >100 | >100 |
0.033 | >0.277 | >0.277 | >0.277 | >0.277 |
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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
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 StylePazderková, Markéta, Václav Profant, Petr Maloň, Rina K. Dukor, Václav Čeřovský, Vladimír Baumruk, and Lucie Bednárová. 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