Biophysical studies of the membrane location of the voltage-gated sensors in the HsapBK and KvAP K+ channels

Henrik Biverståhl, Jesper Lind, A. Bodor, Lena Mäler

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The membrane location of two fragments in two different K+-channels, the KvAP (from Aeropyrum pernix) and the HsapBK (human) corresponding to the putative "paddle" domains, has been investigated by CD, fluorescence and NMR spectroscopy. Both domains interact with q = 0.5 phospholipid bicelles, DHPC micelles and with POPC vesicles. CD spectra demonstrate that both peptides become largely helical in the presence of phospholipid bicelles. Fluorescence quenching studies using soluble acrylamide or lipid-attached doxyl-groups show that the arginine-rich domains are located within the bilayered region in phospholipid bicelles. Nuclear magnetic relaxation parameters, T1 and 13C-1H NOE, for DMPC in DMPC/DHPC bicelles and for DHPC in micelles showed that the lipid acyl chains in the bicelles become less flexible in the presence of either of the fragments. An even more pronounced effect is seen on the glycerol carbons. 2H NMR spectra of magnetically aligned bicelles showed that the peptide derived from KvAP had no or little effect on bilayer order, while the peptide derived from HsapBK had the effect of lowering the order of the bilayer. The present study demonstrates that the fragments derived from the full-length proteins interact with the bilayered interior of model membranes, and that they affect both the local mobility and lipid order of model membrane systems.

Original languageEnglish
Pages (from-to)1976-1986
Number of pages11
JournalBBA - Biomembranes
Volume1788
Issue number9
DOIs
Publication statusPublished - Sep 2009

Fingerprint

Dimyristoylphosphatidylcholine
Phospholipids
Micelles
Membranes
Lipids
Peptides
Aeropyrum
Sensors
Electric potential
Magnetic relaxation
Acrylamide
Fluorescence Spectrometry
Fluorescence spectroscopy
Glycerol
Nuclear magnetic resonance spectroscopy
Arginine
Quenching
Magnetic Resonance Spectroscopy
Carbon
Fluorescence

Keywords

  • Bicelle
  • Fluorescence
  • K-channel
  • Membrane
  • Micelle
  • NMR
  • Voltage-sensor

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Biophysics

Cite this

Biophysical studies of the membrane location of the voltage-gated sensors in the HsapBK and KvAP K+ channels. / Biverståhl, Henrik; Lind, Jesper; Bodor, A.; Mäler, Lena.

In: BBA - Biomembranes, Vol. 1788, No. 9, 09.2009, p. 1976-1986.

Research output: Contribution to journalArticle

Biverståhl, Henrik ; Lind, Jesper ; Bodor, A. ; Mäler, Lena. / Biophysical studies of the membrane location of the voltage-gated sensors in the HsapBK and KvAP K+ channels. In: BBA - Biomembranes. 2009 ; Vol. 1788, No. 9. pp. 1976-1986.
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