RT Journal Article
T1 Effects of Ca2+ ions on bestrophin-1 surface films.
A1 Mladenova, Kirilka
A1 Petrova, Svetla D
A1 Andreeva, Tonya D
A1 Moskova-Doumanova, Veselina
A1 Topouzova-Hristova, Tanya
A1 Kalvachev, Yuri
A1 Balashev, Konstantin
A1 Bhattacharya, Shomi S
A1 Chakarova, Christina
A1 Lalchev, Zdravko
A1 Doumanov, Jordan A
K1 AFM
K1 BAM
K1 FTIR
K1 Langmuir-Blodgett films
K1 hBest1
K1 π/A isotherms
AB 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.
YR 2016
FD 2016-10-13
LK http://hdl.handle.net/10668/10552
UL http://hdl.handle.net/10668/10552
LA en
DS RISalud
RD Apr 7, 2025