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

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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 et al.

In: Peptide Science, Vol. 110, No. 5, e23083, 09.2018.

Research output: Contribution to journal › Article › peer-review

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

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

Conformational properties, membrane interaction, and antibacterial activity of the peptaibiotic chalciporin a: Multitechnique spectroscopic and biophysical investigations on the natural compound and labeled analogs

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