A Temperature-Driven, Reversible, Helical-Handedness Inversion in Peptaibol Analogues Tuned by the C-Terminal Capping Moiety

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A Temperature-Driven, Reversible, Helical-Handedness Inversion in Peptaibol Analogues Tuned by the C-Terminal Capping Moiety. / De Zotti, Marta; Syryamina, Victoria N.; Hussain, Rohanah et al.

In: ChemBioChem, Vol. 20, No. 16, 16.08.2019, p. 2125-2132.

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

BibTeX

@article{6c7072a2aa7145ba8992094fad2bd4ee,

title = "A Temperature-Driven, Reversible, Helical-Handedness Inversion in Peptaibol Analogues Tuned by the C-Terminal Capping Moiety",

abstract = "Trichogin is a natural peptide endowed with antimicrobial and antitumor activity. A member of the peptaibol family, trichogin possesses a C-terminal amino alcohol. In the past, this moiety was substituted for a methyl ester for synthetic purposes and it was observed that this apparently slight modification caused significant changes in the peptide bioactivity. With the aim of understanding the reasons behind such observations, a detailed spectroscopic study on a number of trichogin analogues has been performed. Herein, data obtained from synchrotron radiation circular dichroism, NMR spectroscopy, and fluorescence spectroscopy in organic solvents at cryogenic temperatures are compared with those independently acquired by means of EPR spectroscopy at 80 K. It is unambiguously revealed that the presence of a reversible, temperature-driven, screw-sense interconversion from a right- to left-handed helix is determined by the C-terminal capping moiety. Data demonstrate, for the first time, the key role of a C-terminal methyl ester in promoting peptide screw-sense inversion.",

keywords = "antimicrobial peptides, conformational analysis, helical structures, screw-sense switching, synchrotron radiation circular dichroism, SCREW-SENSE, LIPOPEPTAIBOL, ANTIBACTERIAL, MEMBRANE INTERACTION, ACHIRAL PEPTIDE, RESONANCE, TRICHOGIN GA IV, ALPHA-AMINO-ACID, CONFORMATIONAL-ANALYSIS, PREFERENCE",

author = "{De Zotti}, Marta and Syryamina, {Victoria N.} and Rohanah Hussain and Edoardo Longo and Giuliano Siligardi and Dzuba, {Sergei A.} and Lorenzo Stella and Fernando Formaggio",

note = "Publisher Copyright: {\textcopyright} 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim",

year = "2019",

month = aug,

day = "16",

doi = "10.1002/cbic.201900235",

language = "English",

volume = "20",

pages = "2125--2132",

journal = "ChemBioChem",

issn = "1439-4227",

publisher = "Wiley-VCH Verlag",

number = "16",

}

RIS

TY - JOUR

T1 - A Temperature-Driven, Reversible, Helical-Handedness Inversion in Peptaibol Analogues Tuned by the C-Terminal Capping Moiety

AU - De Zotti, Marta

AU - Syryamina, Victoria N.

AU - Hussain, Rohanah

AU - Longo, Edoardo

AU - Siligardi, Giuliano

AU - Dzuba, Sergei A.

AU - Stella, Lorenzo

AU - Formaggio, Fernando

PY - 2019/8/16

Y1 - 2019/8/16

N2 - Trichogin is a natural peptide endowed with antimicrobial and antitumor activity. A member of the peptaibol family, trichogin possesses a C-terminal amino alcohol. In the past, this moiety was substituted for a methyl ester for synthetic purposes and it was observed that this apparently slight modification caused significant changes in the peptide bioactivity. With the aim of understanding the reasons behind such observations, a detailed spectroscopic study on a number of trichogin analogues has been performed. Herein, data obtained from synchrotron radiation circular dichroism, NMR spectroscopy, and fluorescence spectroscopy in organic solvents at cryogenic temperatures are compared with those independently acquired by means of EPR spectroscopy at 80 K. It is unambiguously revealed that the presence of a reversible, temperature-driven, screw-sense interconversion from a right- to left-handed helix is determined by the C-terminal capping moiety. Data demonstrate, for the first time, the key role of a C-terminal methyl ester in promoting peptide screw-sense inversion.

AB - Trichogin is a natural peptide endowed with antimicrobial and antitumor activity. A member of the peptaibol family, trichogin possesses a C-terminal amino alcohol. In the past, this moiety was substituted for a methyl ester for synthetic purposes and it was observed that this apparently slight modification caused significant changes in the peptide bioactivity. With the aim of understanding the reasons behind such observations, a detailed spectroscopic study on a number of trichogin analogues has been performed. Herein, data obtained from synchrotron radiation circular dichroism, NMR spectroscopy, and fluorescence spectroscopy in organic solvents at cryogenic temperatures are compared with those independently acquired by means of EPR spectroscopy at 80 K. It is unambiguously revealed that the presence of a reversible, temperature-driven, screw-sense interconversion from a right- to left-handed helix is determined by the C-terminal capping moiety. Data demonstrate, for the first time, the key role of a C-terminal methyl ester in promoting peptide screw-sense inversion.

KW - antimicrobial peptides

KW - conformational analysis

KW - helical structures

KW - screw-sense switching

KW - synchrotron radiation circular dichroism

KW - SCREW-SENSE

KW - LIPOPEPTAIBOL

KW - ANTIBACTERIAL

KW - MEMBRANE INTERACTION

KW - ACHIRAL PEPTIDE

KW - RESONANCE

KW - TRICHOGIN GA IV

KW - ALPHA-AMINO-ACID

KW - CONFORMATIONAL-ANALYSIS

KW - PREFERENCE

UR - http://www.scopus.com/inward/record.url?scp=85068895370&partnerID=8YFLogxK

U2 - 10.1002/cbic.201900235

DO - 10.1002/cbic.201900235

M3 - Article

C2 - 31095838

AN - SCOPUS:85068895370

VL - 20

SP - 2125

EP - 2132

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

IS - 16

ER -

ID: 20850177