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

التفاصيل البيبلوغرافية
العنوان: Interaction between soluble and membrane-embedded potassium channel peptides monitored by Fourier transform infrared spectroscopy.
المؤلفون: Geoffrey W Abbott, Bala Ramesh, Surjit K Srai
المصدر: PLoS ONE, Vol 7, Iss 11, p e49070 (2012)
بيانات النشر: Public Library of Science (PLoS), 2012.
سنة النشر: 2012
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: 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.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
Relation: http://europepmc.org/articles/PMC3493504?pdf=render; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0049070
URL الوصول: https://doaj.org/article/c6f2194a0b6447cba71ddcd8ba31f051
رقم الأكسشن: edsdoj.6f2194a0b6447cba71ddcd8ba31f051
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0049070