Vanin-1 is an amidohydrolase that catalyses the conversion of pantetheine into the amino-thiol cysteamine and pantothenic acid (coenzyme A precursor), which plays a vital role in multiple physiological and pathological processes. In this study, an enzyme-activated near-infrared (NIR) fluorescent probe (DDAV) has been constructed for sensitively detecting Vanin-1 activity in complicated biosamples on the basis of its catalytic characteristics. DDAV exhibited a high selectivity and sensitivity toward Vanin-1 and was successfully applied to the early diagnosis of kidney injury in cisplatin-induced kidney injury model. In addition, DDAV could serve as a visual tool for in situ imaging endogenous Vanin-1 in vivo. More importantly, Enterococcus faecalis 20247 which possessed high expression of Vanin-1 was screened out from intestinal bacteria using DDAV, provided useful guidance for the rational use of NSAIDs in clinic. Finally, oleuropein as a potent natural inhibitor for Vanin-1 was discovered from herbal medicines library using a high-throughput screening method using DDAV, which held great promise for clinical therapy of inflammatory bowel disease.

Vanin-1 是一种酰胺水解酶，可催化泛硫胺酸转化为氨基硫醇半胱胺和泛酸（辅酶 A 前体），在多种生理和病理过程中发挥重要作用。本研究基于其催化特性构建了一种酶激活近红外（NIR）荧光探针（DDAV），用于灵敏检测复杂生物样品中的Vanin-1活性。DDAV对Vanin-1表现出高选择性和敏感性，成功应用于顺铂肾损伤模型肾损伤的早期诊断。此外，DDAV 可以作为一种视觉工具，用于体内原位成像内源性 Vanin-1 。更重要的是，粪肠球菌利用DDAV从肠道细菌中筛选出Vanin-1高表达的20247，为临床合理使用NSAIDs提供了有益的指导。最后，使用DDAV的高通量筛选方法从草药库中发现橄榄苦苷作为Vanin-1的有效天然抑制剂，这对炎症性肠病的临床治疗具有很大的前景。