Ca2+-induced changes of surfactin conformation

AFTIR and circular dichroism study

E. Vass, Zs. Majer, M. Hollósi, L. Volpon, M. Hollósi

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Previous NMR studies on surfactin proposed two γ orβ-turn-containing conformers while recent CD studies describedβ-sheets and α-helices in surfactin. Since these datawere not obtained in the same conditions, the conformation ofsurfactin was reinvestigated by FTIR spectroscopy, a diagnosticmethod for β-sheets. In trifluoroethanol, the FTIR spectra ofsurfactin and its diester are compatible with γ and/orβ-turn(s) and the differences in their CD spectra show theimportance of the Glu1 and Asp5 COOH groupsin stabilizing the lipopeptide conformation. The calcium-inducedspectral changes of both lipopeptides suggest a first binding ofthe divalent ions to the surfactin COOH groups (untilcalcium-lipopeptide mole ratio reached 1) followed by bulkconformational changes (at higher mole ratios). In Tris buffer atpH 8.5, the FTIR amide I band shape, without the typical 1610-1628and 1675-1695 cm-1 bands, ascertains the absence ofβ-sheets.

Original languageEnglish
Pages (from-to)361-367
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume282
Issue number1
DOIs
Publication statusPublished - 2001

Fingerprint

Lipopeptides
Fourier Transform Infrared Spectroscopy
Circular Dichroism
Conformations
Trifluoroethanol
Tromethamine
Amides
Spectrum Analysis
Nuclear magnetic resonance
Spectroscopy
Ions
Calcium

Keywords

  • Circular dichroism
  • Conformation
  • Fourier transforminfrared
  • Surfactin
  • Turns

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Ca2+-induced changes of surfactin conformation : AFTIR and circular dichroism study. / Vass, E.; Majer, Zs.; Hollósi, M.; Volpon, L.; Hollósi, M.

In: Biochemical and Biophysical Research Communications, Vol. 282, No. 1, 2001, p. 361-367.

Research output: Contribution to journalArticle

@article{25cabc78a6f24fd5b335bcdb3affd9d9,
title = "Ca2+-induced changes of surfactin conformation: AFTIR and circular dichroism study",
abstract = "Previous NMR studies on surfactin proposed two γ orβ-turn-containing conformers while recent CD studies describedβ-sheets and α-helices in surfactin. Since these datawere not obtained in the same conditions, the conformation ofsurfactin was reinvestigated by FTIR spectroscopy, a diagnosticmethod for β-sheets. In trifluoroethanol, the FTIR spectra ofsurfactin and its diester are compatible with γ and/orβ-turn(s) and the differences in their CD spectra show theimportance of the Glu1 and Asp5 COOH groupsin stabilizing the lipopeptide conformation. The calcium-inducedspectral changes of both lipopeptides suggest a first binding ofthe divalent ions to the surfactin COOH groups (untilcalcium-lipopeptide mole ratio reached 1) followed by bulkconformational changes (at higher mole ratios). In Tris buffer atpH 8.5, the FTIR amide I band shape, without the typical 1610-1628and 1675-1695 cm-1 bands, ascertains the absence ofβ-sheets.",
keywords = "Circular dichroism, Conformation, Fourier transforminfrared, Surfactin, Turns",
author = "E. Vass and Zs. Majer and M. Holl{\'o}si and L. Volpon and M. Holl{\'o}si",
year = "2001",
doi = "10.1006/bbrc.2001.4469",
language = "English",
volume = "282",
pages = "361--367",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Ca2+-induced changes of surfactin conformation

T2 - AFTIR and circular dichroism study

AU - Vass, E.

AU - Majer, Zs.

AU - Hollósi, M.

AU - Volpon, L.

AU - Hollósi, M.

PY - 2001

Y1 - 2001

N2 - Previous NMR studies on surfactin proposed two γ orβ-turn-containing conformers while recent CD studies describedβ-sheets and α-helices in surfactin. Since these datawere not obtained in the same conditions, the conformation ofsurfactin was reinvestigated by FTIR spectroscopy, a diagnosticmethod for β-sheets. In trifluoroethanol, the FTIR spectra ofsurfactin and its diester are compatible with γ and/orβ-turn(s) and the differences in their CD spectra show theimportance of the Glu1 and Asp5 COOH groupsin stabilizing the lipopeptide conformation. The calcium-inducedspectral changes of both lipopeptides suggest a first binding ofthe divalent ions to the surfactin COOH groups (untilcalcium-lipopeptide mole ratio reached 1) followed by bulkconformational changes (at higher mole ratios). In Tris buffer atpH 8.5, the FTIR amide I band shape, without the typical 1610-1628and 1675-1695 cm-1 bands, ascertains the absence ofβ-sheets.

AB - Previous NMR studies on surfactin proposed two γ orβ-turn-containing conformers while recent CD studies describedβ-sheets and α-helices in surfactin. Since these datawere not obtained in the same conditions, the conformation ofsurfactin was reinvestigated by FTIR spectroscopy, a diagnosticmethod for β-sheets. In trifluoroethanol, the FTIR spectra ofsurfactin and its diester are compatible with γ and/orβ-turn(s) and the differences in their CD spectra show theimportance of the Glu1 and Asp5 COOH groupsin stabilizing the lipopeptide conformation. The calcium-inducedspectral changes of both lipopeptides suggest a first binding ofthe divalent ions to the surfactin COOH groups (untilcalcium-lipopeptide mole ratio reached 1) followed by bulkconformational changes (at higher mole ratios). In Tris buffer atpH 8.5, the FTIR amide I band shape, without the typical 1610-1628and 1675-1695 cm-1 bands, ascertains the absence ofβ-sheets.

KW - Circular dichroism

KW - Conformation

KW - Fourier transforminfrared

KW - Surfactin

KW - Turns

UR - http://www.scopus.com/inward/record.url?scp=0034804846&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034804846&partnerID=8YFLogxK

U2 - 10.1006/bbrc.2001.4469

DO - 10.1006/bbrc.2001.4469

M3 - Article

VL - 282

SP - 361

EP - 367

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -