Author: Brian G. Pierce; Zhen-Yong Keck; Ruixue Wang; Patrick Lau; Kyle Garagusi; Khadija Elkholy; Eric A. Toth; Richard A. Urbanowicz; Johnathan D. Guest; Pragati Agnihotri; Melissa C. Kerzic; Alexander Marin; Alexander K. Andrianov; Jonathan K. Ball; Roy A. Mariuzza; Thomas R. Fuerst; Steven K.H. Foung
Title: Structure-based design of hepatitis C virus E2 glycoprotein improves serum binding and cross-neutralization Document date: 2020_4_17
ID: b6to1v4u_55
Snippet: The interaction of recombinant sE2 glycoproteins with CD81 and HMAbs in was measured using an Octet RED96 instrument and Ni 2+ -NTA biosensors (Pall ForteBio). The biosensors were loaded with 5 ïg/mL of purified His6-tagged wild-type or mutant sE2 for 600 sec. Association for 300 sec followed by dissociation for 300 sec against a 2-fold concentration dilution series of each antibody was performed. Data analysis was performed using Octet Data An.....
Document: The interaction of recombinant sE2 glycoproteins with CD81 and HMAbs in was measured using an Octet RED96 instrument and Ni 2+ -NTA biosensors (Pall ForteBio). The biosensors were loaded with 5 ïg/mL of purified His6-tagged wild-type or mutant sE2 for 600 sec. Association for 300 sec followed by dissociation for 300 sec against a 2-fold concentration dilution series of each antibody was performed. Data analysis was performed using Octet Data Analysis 10.0 software and utilized reference subtraction at 0 nM antibody concentration, alignment to the baseline, interstep correction to the dissociation step, and Savitzky-Golay fitting. Curves were globally fitted based on association and dissociation to obtain KD values.
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