Oligomerization status and surface hydrophobicity of αB-lir hybrid protein.
figureposted on 2022-05-02, 17:25 authored by Samaneh Ahmadi, Mohammad Bagher Shahsavani, Zohreh Tavaf, Rawayh Muslim Albaghlany, Ashutosh Kumar, Ali Akbar Moosavi-Movahedi, Reza Yousefi
A) The hydrodynamic diameters of αB-lir hybrid protein and human αB-Cry (1 mg/mL in phosphate buffer, pH 7.4) were measured at different temperatures by a DLS instrument. B) For the ANS fluorescence assessments, the αB-lir and αB-Cry were prepared in 50 mM sodium phosphate buffer, pH 7.4 and the protein concentrations were fixed at 0.15 mg/mL. Then, their surface hydrophobicity analyses were performed at various temperatures in the presence of a fixed ANS concentration (100 μM). The excitation of the protein/ANS complex was done at 365 nm, and the emission spectra were collected between 400–600 nm. Also, the excitation and emission slits were fixed at 5 and 10 nm, respectively .
Read the peer-reviewed publication
stimulated insulin secretionrelatively good efficiencygel filtration chromatographyescherichia coli </blood sugar levelsanion exchange chromatographysheet rich structuresecondary structures suggestedrelatively longer periodpresent study aimedprecipitation method followedmass spectroscopy analysisacting incretin mimicliraglutide precursor peptidediv >< phybrid protein exertsstudy suggestedhybrid proteinnovel methodmolecular masslonger halfincretin mimicshelical structurecarrier proteinsubcutaneous injectionsmall numbernovel strategynew longhplc estimatedgene levelgene constructfinally confirmeddominant αdiabetic mice98 %.70 %.