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用于在学术和商业环境中轻松、快速测定蛋白质稳定性的新型微尺度方法。

Novel microscale approaches for easy, rapid determination of protein stability in academic and commercial settings.

作者信息

Alexander Crispin G, Wanner Randy, Johnson Christopher M, Breitsprecher Dennis, Winter Gerhard, Duhr Stefan, Baaske Philipp, Ferguson Neil

机构信息

School of Medicine and Medical Science, University College Dublin, Dublin 4, Ireland.

Department of Pharmacy, Pharmaceutical Technology and Biopharmaceutics, LMU Munich, Butenandtstr. 5, 81377 Munich, Germany; NanoTemper Technologies GmbH, Floessergasse 4, 81369 Munich, Germany.

出版信息

Biochim Biophys Acta. 2014 Dec;1844(12):2241-50. doi: 10.1016/j.bbapap.2014.09.016. Epub 2014 Sep 28.

Abstract

Chemical denaturant titrations can be used to accurately determine protein stability. However, data acquisition is typically labour intensive, has low throughput and is difficult to automate. These factors, combined with high protein consumption, have limited the adoption of chemical denaturant titrations in commercial settings. Thermal denaturation assays can be automated, sometimes with very high throughput. However, thermal denaturation assays are incompatible with proteins that aggregate at high temperatures and large extrapolation of stability parameters to physiological temperatures can introduce significant uncertainties. We used capillary-based instruments to measure chemical denaturant titrations by intrinsic fluorescence and microscale thermophoresis. This allowed higher throughput, consumed several hundred-fold less protein than conventional, cuvette-based methods yet maintained the high quality of the conventional approaches. We also established efficient strategies for automated, direct determination of protein stability at a range of temperatures via chemical denaturation, which has utility for characterising stability for proteins that are difficult to purify in high yield. This approach may also have merit for proteins that irreversibly denature or aggregate in classical thermal denaturation assays. We also developed procedures for affinity ranking of protein-ligand interactions from ligand-induced changes in chemical denaturation data, and proved the principle for this by correctly ranking the affinity of previously unreported peptide-PDZ domain interactions. The increased throughput, automation and low protein consumption of protein stability determinations afforded by using capillary-based methods to measure denaturant titrations, can help to revolutionise protein research. We believe that the strategies reported are likely to find wide applications in academia, biotherapeutic formulation and drug discovery programmes.

摘要

化学变性剂滴定可用于准确测定蛋白质稳定性。然而,数据采集通常劳动强度大、通量低且难以自动化。这些因素,再加上蛋白质消耗量大,限制了化学变性剂滴定在商业环境中的应用。热变性分析可以自动化,有时通量非常高。然而,热变性分析与在高温下聚集的蛋白质不兼容,并且将稳定性参数大量外推到生理温度会引入显著的不确定性。我们使用基于毛细管的仪器通过内在荧光和微量热泳测定化学变性剂滴定。这实现了更高的通量,与基于比色皿的传统方法相比,蛋白质消耗量减少了数百倍,同时保持了传统方法的高质量。我们还建立了通过化学变性在一系列温度下自动、直接测定蛋白质稳定性的有效策略,这对于表征难以高产纯化的蛋白质的稳定性很有用。这种方法对于在经典热变性分析中不可逆变性或聚集的蛋白质也可能有价值。我们还开发了从配体诱导的化学变性数据变化中对蛋白质 - 配体相互作用进行亲和力排序的程序,并通过正确排序先前未报道的肽 - PDZ 结构域相互作用的亲和力证明了这一原理。使用基于毛细管的方法测量变性剂滴定所提供的蛋白质稳定性测定的通量增加、自动化和低蛋白质消耗,有助于彻底改变蛋白质研究。我们相信所报道的策略可能会在学术界、生物治疗制剂和药物发现项目中得到广泛应用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/19c4/4332417/c34fda7d971b/fx1.jpg

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