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Title: Effects of Ca2+ ions on bestrophin-1 surface films.
Authors: Mladenova, Kirilka
Petrova, Svetla D
Andreeva, Tonya D
Moskova-Doumanova, Veselina
Topouzova-Hristova, Tanya
Kalvachev, Yuri
Balashev, Konstantin
Bhattacharya, Shomi S
Chakarova, Christina
Lalchev, Zdravko
Doumanov, Jordan A
Keywords: AFM;BAM;FTIR;Langmuir-Blodgett films;hBest1;π/A isotherms
metadata.dc.subject.mesh: Animals
Cations, Divalent
Chloride Channels
Eye Proteins
Gene Expression
Madin Darby Canine Kidney Cells
Membranes, Artificial
Protein Structure, Secondary
Recombinant Proteins
Surface Properties
Issue Date: 13-Oct-2016
Abstract: Human bestrophin-1 (hBest1) is a transmembrane calcium-activated chloride channel protein - member of the bestrophin family of anion channels, predominantly expressed in the membrane of retinal pigment epithelium (RPE) cells. Mutations in the protein cause ocular diseases, named Bestrophinopathies. Here, we present the first Fourier transform infrared (FTIR) study of the secondary structure elements of hBest1, π/A isotherms and hysteresis, Brewster angle microscopy (BAM) and atomic force microscopy (AFM) visualization of the aggregation state of protein molecules dispersed as Langmuir and Langmuir-Blodgett films. The secondary structure of hBest1 consists predominantly of 310-helices (27.2%), α-helixes (16.3%), β-turns and loops (32.2%). AFM images of hBest1 suggest approximate lateral dimensions of 100×160Å and 75Å height. Binding of calcium ions (Ca2+) induces conformational changes in the protein secondary structure leading to assembly of protein molecules and changes in molecular and macro-organization of hBest1 in monolayers. These data provide basic information needed in pursuit of molecular mechanisms underlying retinal and other pathologies linked to this protein.
metadata.dc.identifier.doi: 10.1016/j.colsurfb.2016.10.023
Appears in Collections:Producción 2020

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