Abstract
The properties of antimicrobial peptides adsorbed on inorganic or organic surfaces are of interest for their potential applications in intracellular drug delivery. In this work, continuous-wave (CW) electron paramagnetic resonance (EPR) and pulsed electron-electron double resonance (PELDOR) techniques were applied to study adsorption of the short-sequence trichogin GA IV and the medium-length sequence ampullosporin A antimicrobial peptides on the monodisperse colloidal silica nanospheres of 20 nm diameter. The results obtained by CW EPR support the view that the adsorbed peptides form close-packed clusters. PELDOR data show that both trichogin and ampullosporin adsorbed on the silica surface possess a more disordered conformation as compared to that in solution. For ampullosporin, disordering is much more pronounced than for trichogin. After desorption, the peptides restored their conformations; upon adsorption the peptides in some cases may lose partly their biradical character.
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Acknowledgments
We thank Dr. A.D. Milov for helpful discussion and assistance in some of the measurements. This work was supported by the Russian Science Foundation, project no. 15-15-00021.
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Syryamina, V.N., Samoilova, R.I., Tsvetkov, Y.D. et al. Peptides on the Surface: Spin-Label EPR and PELDOR Study of Adsorption of the Antimicrobial Peptides Trichogin GA IV and Ampullosporin A on the Silica Nanoparticles. Appl Magn Reson 47, 309–320 (2016). https://doi.org/10.1007/s00723-015-0745-5
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DOI: https://doi.org/10.1007/s00723-015-0745-5