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

在这项研究中，首次报道了在与唾液肽组蛋白 3 结合时改变结构构象的单链 DNA 适体。Histatin 3 是一种抗菌肽，具有作为口腔念珠菌病治疗剂的能力，最近被认为是急性应激的新型生物标志物。通过体外迭代的文库固定版本鉴定适体称为指数富集配体系统进化 (SELEX) 的过程。通过 SELEX 过程，确定了四个共享一致序列的独特适体候选者。这些选定的序列表现出对组蛋白 3 的结合亲和力和特异性，为了进一步表征这些适体，开发了直接形式酶联适体吸附测定 (ELASA)。表现最佳的候选者表现出1.97 ± 0.48 μM的平衡解离常数 ( K _d ) 值。这些新型适体有可能导致进一步开发用于检测和量化人类唾液和其他生物介质中组蛋白 3 的精细传感分析和平台。