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Conformational properties, membrane interaction, and antibacterial activity of the peptaibiotic chalciporin a : Multitechnique spectroscopic and biophysical investigations on the natural compound and labeled analogs. / Biondi, Barbara; Peggion, Cristina; De Zotti, Marta и др.

в: Peptide Science, Том 110, № 5, e23083, 09.2018.

Результаты исследований: Научные публикации в периодических изданияхстатьяРецензирование

Harvard

Biondi, B, Peggion, C, De Zotti, M, Pignaffo, C, Dalzini, A, Bortolus, M, Oancea, S, Hilma, G, Bortolotti, A, Stella, L, Pedersen, JZ, Syryamina, VN, Tsvetkov, YD, Dzuba, SA, Toniolo, C & Formaggio, F 2018, 'Conformational properties, membrane interaction, and antibacterial activity of the peptaibiotic chalciporin a: Multitechnique spectroscopic and biophysical investigations on the natural compound and labeled analogs', Peptide Science, Том. 110, № 5, e23083. https://doi.org/10.1002/bip.23083

APA

Biondi, B., Peggion, C., De Zotti, M., Pignaffo, C., Dalzini, A., Bortolus, M., Oancea, S., Hilma, G., Bortolotti, A., Stella, L., Pedersen, J. Z., Syryamina, V. N., Tsvetkov, Y. D., Dzuba, S. A., Toniolo, C., & Formaggio, F. (2018). Conformational properties, membrane interaction, and antibacterial activity of the peptaibiotic chalciporin a: Multitechnique spectroscopic and biophysical investigations on the natural compound and labeled analogs. Peptide Science, 110(5), [e23083]. https://doi.org/10.1002/bip.23083

Vancouver

Biondi B, Peggion C, De Zotti M, Pignaffo C, Dalzini A, Bortolus M и др. Conformational properties, membrane interaction, and antibacterial activity of the peptaibiotic chalciporin a: Multitechnique spectroscopic and biophysical investigations on the natural compound and labeled analogs. Peptide Science. 2018 сент.;110(5):e23083. Epub 2017 нояб. 11. doi: 10.1002/bip.23083

Author

BibTeX

@article{28b74dc12f484985994f4912aa2285da,
title = "Conformational properties, membrane interaction, and antibacterial activity of the peptaibiotic chalciporin a: Multitechnique spectroscopic and biophysical investigations on the natural compound and labeled analogs",
abstract = "In this work, an extensive set of spectroscopic and biophysical techniques (including FT-IR absorption, CD, 2D-NMR, fluorescence, and CW/PELDOR EPR) was used to study the conformational preferences, membrane interaction, and bioactivity properties of the naturally occurring synthetic 14-mer peptaibiotic chalciporin A, characterized by a relatively low (≈20%), uncommon proportion of the strongly helicogenic Aib residue. In addition to the unlabeled peptide, we gained in-depth information from the study of two labeled analogs, characterized by one or two residues of the helicogenic, nitroxyl radical-containing TOAC. All three compounds were prepared using the SPPS methodology, which was carefully modified in the course of the syntheses of TOAC-labeled analogs in view of the poorly reactive a-amino function of this very bulky residue and the specific requirements of its free-radical side chain. Despite its potentially high flexibility, our results point to a predominant, partly amphiphilic, a-helical conformation for this peptaibiotic. Therefore, not surprisingly, we found an effective membrane affinity and a remarkable penetration propensity. However, chalciporin A exhibits a selectivity in its antibacterial activity not in agreement with that typical of the other members of this peptide class.",
keywords = "Biological activity, Chalciporin, Conformation, Membrane penetration, Peptaibiotics, membrane penetration, TRYPTOPHAN, biological activity, peptaibiotics, VIBRATIONAL CIRCULAR-DICHROISM, chalciporin, conformation, ANTIMICROBIAL PEPTIDES, PREFERRED CONFORMATION, AMPULLOSPORIN, TRICHOGIN GA-IV, MEDIUM-LENGTH, ALPHA-AMINO-ACID, TOAC, CHAIN-LENGTH",
author = "Barbara Biondi and Cristina Peggion and {De Zotti}, Marta and Chiara Pignaffo and Annalisa Dalzini and Marco Bortolus and Simona Oancea and Geta Hilma and Annalisa Bortolotti and Lorenzo Stella and Pedersen, {Jens Z.} and Syryamina, {Victoria N.} and Tsvetkov, {Yuri D.} and Dzuba, {Sergei A.} and Claudio Toniolo and Fernando Formaggio",
note = "Publisher Copyright: {\textcopyright} 2017VC Wiley Periodicals, Inc. . ",
year = "2018",
month = sep,
doi = "10.1002/bip.23083",
language = "English",
volume = "110",
journal = "Peptide Science",
issn = "2475-8817",
publisher = "John Wiley & Sons Inc.",
number = "5",

}

RIS

TY - JOUR

T1 - Conformational properties, membrane interaction, and antibacterial activity of the peptaibiotic chalciporin a

T2 - Multitechnique spectroscopic and biophysical investigations on the natural compound and labeled analogs

AU - Biondi, Barbara

AU - Peggion, Cristina

AU - De Zotti, Marta

AU - Pignaffo, Chiara

AU - Dalzini, Annalisa

AU - Bortolus, Marco

AU - Oancea, Simona

AU - Hilma, Geta

AU - Bortolotti, Annalisa

AU - Stella, Lorenzo

AU - Pedersen, Jens Z.

AU - Syryamina, Victoria N.

AU - Tsvetkov, Yuri D.

AU - Dzuba, Sergei A.

AU - Toniolo, Claudio

AU - Formaggio, Fernando

N1 - Publisher Copyright: © 2017VC Wiley Periodicals, Inc. .

PY - 2018/9

Y1 - 2018/9

N2 - In this work, an extensive set of spectroscopic and biophysical techniques (including FT-IR absorption, CD, 2D-NMR, fluorescence, and CW/PELDOR EPR) was used to study the conformational preferences, membrane interaction, and bioactivity properties of the naturally occurring synthetic 14-mer peptaibiotic chalciporin A, characterized by a relatively low (≈20%), uncommon proportion of the strongly helicogenic Aib residue. In addition to the unlabeled peptide, we gained in-depth information from the study of two labeled analogs, characterized by one or two residues of the helicogenic, nitroxyl radical-containing TOAC. All three compounds were prepared using the SPPS methodology, which was carefully modified in the course of the syntheses of TOAC-labeled analogs in view of the poorly reactive a-amino function of this very bulky residue and the specific requirements of its free-radical side chain. Despite its potentially high flexibility, our results point to a predominant, partly amphiphilic, a-helical conformation for this peptaibiotic. Therefore, not surprisingly, we found an effective membrane affinity and a remarkable penetration propensity. However, chalciporin A exhibits a selectivity in its antibacterial activity not in agreement with that typical of the other members of this peptide class.

AB - In this work, an extensive set of spectroscopic and biophysical techniques (including FT-IR absorption, CD, 2D-NMR, fluorescence, and CW/PELDOR EPR) was used to study the conformational preferences, membrane interaction, and bioactivity properties of the naturally occurring synthetic 14-mer peptaibiotic chalciporin A, characterized by a relatively low (≈20%), uncommon proportion of the strongly helicogenic Aib residue. In addition to the unlabeled peptide, we gained in-depth information from the study of two labeled analogs, characterized by one or two residues of the helicogenic, nitroxyl radical-containing TOAC. All three compounds were prepared using the SPPS methodology, which was carefully modified in the course of the syntheses of TOAC-labeled analogs in view of the poorly reactive a-amino function of this very bulky residue and the specific requirements of its free-radical side chain. Despite its potentially high flexibility, our results point to a predominant, partly amphiphilic, a-helical conformation for this peptaibiotic. Therefore, not surprisingly, we found an effective membrane affinity and a remarkable penetration propensity. However, chalciporin A exhibits a selectivity in its antibacterial activity not in agreement with that typical of the other members of this peptide class.

KW - Biological activity

KW - Chalciporin

KW - Conformation

KW - Membrane penetration

KW - Peptaibiotics

KW - membrane penetration

KW - TRYPTOPHAN

KW - biological activity

KW - peptaibiotics

KW - VIBRATIONAL CIRCULAR-DICHROISM

KW - chalciporin

KW - conformation

KW - ANTIMICROBIAL PEPTIDES

KW - PREFERRED CONFORMATION

KW - AMPULLOSPORIN

KW - TRICHOGIN GA-IV

KW - MEDIUM-LENGTH

KW - ALPHA-AMINO-ACID

KW - TOAC

KW - CHAIN-LENGTH

UR - http://www.scopus.com/inward/record.url?scp=85078172104&partnerID=8YFLogxK

U2 - 10.1002/bip.23083

DO - 10.1002/bip.23083

M3 - Article

C2 - 29127716

AN - SCOPUS:85078172104

VL - 110

JO - Peptide Science

JF - Peptide Science

SN - 2475-8817

IS - 5

M1 - e23083

ER -

ID: 25831380