Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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. / Syryamina, Victoria N.; Samoilova, Rimma I.; Tsvetkov, Yuri D. и др.
в: Applied Magnetic Resonance, Том 47, № 3, 01.03.2016, стр. 309-320.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Peptides on the Surface
T2 - Spin-Label EPR and PELDOR Study of Adsorption of the Antimicrobial Peptides Trichogin GA IV and Ampullosporin A on the Silica Nanoparticles
AU - Syryamina, Victoria N.
AU - Samoilova, Rimma I.
AU - Tsvetkov, Yuri D.
AU - Ischenko, Arkady V.
AU - De Zotti, Marta
AU - Gobbo, Marina
AU - Toniolo, Claudio
AU - Formaggio, Fernando
AU - Dzuba, Sergei A.
PY - 2016/3/1
Y1 - 2016/3/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84958749883&partnerID=8YFLogxK
U2 - 10.1007/s00723-015-0745-5
DO - 10.1007/s00723-015-0745-5
M3 - Article
AN - SCOPUS:84958749883
VL - 47
SP - 309
EP - 320
JO - Applied Magnetic Resonance
JF - Applied Magnetic Resonance
SN - 0937-9347
IS - 3
ER -
ID: 25831558