Effect of whey protein isolate on the stability and antioxidant capacity of blueberry anthocyanins: A mechanistic and in vitro simulation study
FOOD CHEMISTRY
Authors: Zang, Zhihuan; Chou, Shurui; Tian, Jinlong; Lang, Yuxi; Shen, Yixiao; Ran, Xulong; Gao, Ningxuan; Li, Bin
Abstract
The processing stability and antioxidant capacity of blueberry anthocyanins (ANs) in the presence of whey protein isolate (WPI) were examined. WPI was found to enhance both the stability and antioxidant activity of ANs during processing and simulated in vitro digestion, especially at a concentration of 0.15 mgmL(-1). Fluorescence and ultraviolet-visible absorption spectroscopy showed that ANs were primarily stabilized by hydrophobic forces between WPI and malvidin-3-O-galactoside (M3G), the major anthocyanin monomer. Circular dichroism and Fourier-transform infrared spectroscopy confirmed that the structure of WPI changed and the microenvironments of certain amino acid residues were modulated by non-covalent binding to M3G; furthermore, fewer alpha-helices and more beta-sheets were formed. Molecular docking studies revealed that WPI, especially immunoglobulin (IgG), contributed the most to ANs stability via hydrogen bonds and hydrophobic forces according to molecular docking scores ( - 141.30 kcal/mol). These results provided an important fundamental basis for improving the stabilities of ANs in milk systems.
Affimer-based impedimetric biosensors for fibroblast growth factor receptor 3 (FGFR3): a novel tool for detection and surveillance of recurrent bladder cancer
SENSORS AND ACTUATORS B-CHEMICAL
Authors: Thangsunan, Pattanapong; Lal, Nidhi; Tiede, Christian; Moul, Sophie; Robinson, James, I; Knowles, Margaret A.; Stockley, Peter G.; Beales, Paul A.; Tomlinson, Darren C.; McPherson, Michael J.; Millner, Paul A.
Abstract
Fibroblast growth factor receptor 3 (FGFR3) is a transmembrane tyrosine kinase protein in the fibroblast growth factor receptor family, which plays a key role in many biological processes. Over-expression and activating mutations in FGFR3 are frequent in non-invasive bladder cancer, highlighting this protein as a potential biomarker for recurrent bladder cancer detection. Affimer reagents isolated against recombinant FGFR3 were assessed for their affinity using double-sandwich ELISA and SPR. Anti-FGFR3-14 and FGFR3-21 Affimer proteins showed strong binding to FGFR3 and were used for fabrication of impedimetric electrochemical biosensors. A decrease in impedance was observed when the sensors were exposed to increasing concentrations of FGFR3. The successful impedimetric biosensors were capable of detecting sub-pM to nM concentrations of recombinant FGFR3 protein in phosphate buffered saline as well as in synthetic urine.
COA
Publication 
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