Genome Inspired G-quadruplex DNA Binding Ligands for Affinity MALDI-TOF Mass Spectrometry

摘要

Both insulin and IGF-2 show specific affinity binding with variant a and variant h. The order of binding strength is shown in the following: V-h > V-a > V-i This conclusion was also confirmed by their dissociation constants toward insulin and IGF-2 obtained by surface plasmon resonance study. IGF-2 shows stronger affinity binding toward both variants a and h than insulin. Both variants a and h can capture insulin and IGF-2 from HS at the nM scale. Even though the proteins may exhibit non-specific binding to variant i and untreated silica spots, at lower concentrations their capture is negligible. The difference in protein capture ability is attributed to the ability of variants a and h to form intramolecular G-quadruplex structures.