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Interaction between soluble and membrane-embedded potassium channel peptides monitored by Fourier transform infrared spectroscopy

Abbott, Geoffrey W ; Ramesh, Bala ; Srai, Surjit K Hinderberger, Dariush

PloS one, 2012-11, Vol.7 (11), p.e49070-e49070 [Periódico revisado por pares]

United States: Public Library of Science

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Título:
Interaction between soluble and membrane-embedded potassium channel peptides monitored by Fourier transform infrared spectroscopy
Autor: Abbott, Geoffrey W ; Ramesh, Bala ; Srai, Surjit K
Hinderberger, Dariush
Assuntos: Binding sites ; Biochemistry ; Biology ; Chemistry ; Cooling ; Crystal structure ; Crystallinity ; Crystallography ; Deactivation ; Dimyristoylphosphatidylcholine - chemistry ; Electrostatic properties ; Extrusion ; Fourier transforms ; Helicity ; Hydrogen ; Hydrogen Bonding ; Hydrogen bonds ; Inactivation ; Infrared spectroscopy ; Lecithin ; Lipid Bilayers - chemistry ; Lipid Bilayers - metabolism ; Lipids ; Liquid crystals ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Molecular biology ; Peptides ; Peptides - chemical synthesis ; Peptides - chemistry ; Peptides - metabolism ; Phosphatidylcholine ; Phospholipids ; Physics ; Polypeptides ; Potassium ; Potassium channels ; Potassium channels (voltage-gated) ; Protein interaction ; Protein Interaction Maps ; Protein Structure, Tertiary ; Protein-protein interactions ; Proteins ; Salts ; Sensors ; Shaker Superfamily of Potassium Channels - chemistry ; Shaker Superfamily of Potassium Channels - metabolism ; Shaw Potassium Channels - chemistry ; Shaw Potassium Channels - metabolism ; Solubility ; Spectroscopy ; Spectroscopy, Fourier Transform Infrared ; Spectrum analysis ; Studies ; Thin films
É parte de: PloS one, 2012-11, Vol.7 (11), p.e49070-e49070
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
Conceived and designed the experiments: GWA BR SKS. Performed the experiments: GWA BR. Analyzed the data: GWA. Contributed reagents/materials/analysis tools: BR. Wrote the paper: GWA BR SKS.
Competing Interests: The authors have declared that no competing interests exist.
Descrição: Recent studies have explored the utility of Fourier transform infrared spectroscopy (FTIR) in dynamic monitoring of soluble protein-protein interactions. Here, we investigated the applicability of FTIR to detect interaction between synthetic soluble and phospholipid-embedded peptides corresponding to, respectively, a voltage-gated potassium (Kv) channel inactivation domain (ID) and S4-S6 of the Shaker Kv channel (KV1; including the S4-S5 linker "pre-inactivation" ID binding site). KV1 was predominantly α-helical at 30°C when incorporated into dimyristoyl-l-α-phosphatidylcholine (DMPC) bilayers. Cooling to induce a shift in DMPC from liquid crystalline to gel phase reversibly decreased KV1 helicity, and was previously shown to partially extrude a synthetic S4 peptide. While no interaction was detected in liquid crystalline DMPC, upon cooling to induce the DMPC gel phase a reversible amide I peak (1633 cm(-1)) consistent with novel hydrogen bond formation was detected. This spectral shift was not observed for KV1 in the absence of ID (or vice versa), nor when the non-inactivating mutant V7E ID was applied to KV1 under similar conditions. Alteration of salt or redox conditions affected KV1-ID hydrogen bonding in a manner suggesting electrostatic KV1-ID interaction favored by a hairpin conformation for the ID and requiring extrusion of one or more KV1 domains from DMPC, consistent with ID binding to S4-S5. These findings support the utility of FTIR in detecting reversible interactions between soluble and membrane-embedded proteins, with lipid state-sensitivity of the conformation of the latter facilitating control of the interaction.
Editor: United States: Public Library of Science
Idioma: Inglês

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Interaction between soluble and membrane-embedded potassium channel peptides monitored by Fourier transform infrared spectroscopy

Abbott, Geoffrey W ; Ramesh, Bala ; Srai, Surjit K Hinderberger, Dariush

United States: Public Library of Science

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