病毒灭活是安全处理高风险感染性样本的先决条件。 β-丙内酯 (BPL) 是一种已证实具有杀病毒功效的试剂。 BPL 主要与 DNA、RNA 和氨基酸发生反应。后者可能会修饰干扰亲和试剂（例如用于亲和蛋白质组筛选的抗体和适体）的结合特性的抗原蛋白表位。我们研究了 (i) 使用基于适体的亲和蛋白质组平台 SomaScan BPL 处理对血浆样品中蛋白质水平分析的影响，以及 (ii) 使用基于邻近延伸分析的 Olink Target 平台对条件培养基样品中蛋白质检测的影响。在前一种设置中，使用 SomaScan 平台分析了来自卵巢癌 (n = 12) 和良性疾病 (n = 12) 患者的 BPL 处理血浆样本和天然血浆样本。在后者中，使用 Olink Target 平台分析从有 (n = 3) 或无 (n = 3) 抗 CD3 抗体刺激的培养 T 细胞收集的条件培养基样品。通过比较天然状态和 BPL 处理状态、模拟病毒灭活，评估了蛋白质检测中与 BPL 相关的变化，并评估了对可测量组差异的影响。虽然 BPL 处理显着改变了大约三分之一的 SomaScan 测量值，但大多数抗原/适体相互作用仍然不受影响。 BPL 治疗和疾病状态的相互作用，可能会改变群体差异的可检测性，在不到 1% 的目标 (0.6%) 中可观察到。 BPL 对 Olink Target 蛋白质检测的影响也很有限，影响了 3.6% 的检测蛋白质，且没有可观察到的相互作用效应。因此，BPL 处理的效果仅适度干扰不同实验组之间差异蛋白表达的亲和蛋白质组学检测能力。总体而言，结果证明高通量亲和蛋白质组学非常适合使用 BPL 灭活的高风险样品的分析。

Virus inactivation is a prerequisite for safe handling of high-risk infectious samples. β-Propiolactone (BPL) is an established reagent with proven virucidal efficacy. BPL primarily reacts with DNA, RNA, and amino acids. The latter may modify antigenic protein epitopes interfering with binding properties of affinity reagents such as antibodies and aptamers used in affinity proteomic screens. We investigated (i) the impact of BPL treatment on the analysis of protein levels in plasma samples using the aptamer-based affinity proteomic platform SomaScan and (ii) effects on protein detection in conditioned medium samples using the proximity extension assay-based Olink Target platform. In the former setup, BPL-treated and native plasma samples from patients with ovarian cancer (n = 12) and benign diseases (n = 12) were analyzed using the SomaScan platform. In the latter, conditioned media samples collected from cultured T cells with (n = 3) or without (n = 3) anti-CD3 antibody stimulation were analyzed using the Olink Target platform. BPL-related changes in protein detection were evaluated comparing native and BPL-treated states, simulating virus inactivation, and impact on measurable group differences was assessed. While approximately one-third of SomaScan measurements were significantly changed by the BPL treatment, a majority of antigen/aptamer interactions remained unaffected. Interaction effects of BPL treatment and disease state, potentially altering detectability of group differences, were observable for less than one percent of targets (0.6%). BPL effects on protein detection with Olink Target were also limited, affecting 3.6% of detected proteins with no observable interaction effects. Thus, effects of BPL treatment only moderately interfere with affinity proteomic detectability of differential protein expression between different experimental groups. Overall, the results prove high-throughput affinity proteomics well suited for the analysis of high-risk samples inactivated using BPL.