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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. et al.

In: Applied Magnetic Resonance, Vol. 47, No. 3, 01.03.2016, p. 309-320.

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Syryamina VN, Samoilova RI, Tsvetkov YD, Ischenko AV, De Zotti M, Gobbo M 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. Applied Magnetic Resonance. 2016 Mar 1;47(3):309-320. doi: 10.1007/s00723-015-0745-5

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@article{d984367022b34888a762ecf24d7dd845,
title = "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",
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.",
author = "Syryamina, {Victoria N.} and Samoilova, {Rimma I.} and Tsvetkov, {Yuri D.} and Ischenko, {Arkady V.} and {De Zotti}, Marta and Marina Gobbo and Claudio Toniolo and Fernando Formaggio and Dzuba, {Sergei A.}",
year = "2016",
month = mar,
day = "1",
doi = "10.1007/s00723-015-0745-5",
language = "English",
volume = "47",
pages = "309--320",
journal = "Applied Magnetic Resonance",
issn = "0937-9347",
publisher = "Springer-Verlag GmbH and Co. KG",
number = "3",

}

RIS

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