Selection and characterization of structure-switching DNA aptamers for the salivary peptide histatin 3

In this study, single-stranded DNA aptamers that switch structural conformation upon binding to the salivary peptide histatin 3 have been reported for first time. Histatin is an antimicrobial possesses capability of being a therapeutic agent against oral candidiasis and has recently linked as novel biomarker acute stress. The were identified through library immobilization version iterative in vitro process known Systematic Evolution Ligands by EXponential enrichment (SELEX). Through SELEX process, four unique aptamer candidates sharing consensus sequence identified. These selected sequences exhibited affinity specificity order further characterize these aptamers, direct format enzyme-linked sorbent assay (ELASA) was developed. best performing candidate demonstrated equilibrium dissociation constant (Kd) value 1.97 ± 0.48 μM. potential lead development refined sensing assays platforms detection quantification human saliva other biological media.