从Pth1亲和柱中快速分离天然产物肽- trna水解酶抑制剂。

IF 0.7 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
AIMS Molecular Science Pub Date : 2017-01-01 Epub Date: 2017-05-12 DOI:10.3934/molsci.2017.2.175
Harkirat S Sethi, Jessica L Osier, Geordan L Burks, Jennifer F Lamar, Hana McFeeters, Robert L McFeeters
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引用次数: 1

摘要

需要新的抗生素和新的抗生素靶点来对抗细菌耐药性的发展,这种耐药性有可能使人类退回到抗生素出现之前的时代。细菌肽基trna水解酶(Pth1)是一种前景广阔的新型抗生素靶点。虽然在多种天然产物中观察到抑制活性,但生物活性分离一直是抑制剂分离的瓶颈。为了加速从复杂混合物中分离抑制化合物,我们构建了Pth1亲和柱,并使用它从天然产物中分离抑制化合物。重组产生的鼠伤寒沙门氏菌Pth1共价附着于柱基质上,并从小鼠尾草乙醇提取物中分离出抑制活性。本文报道的过程表明,从复杂的天然产物提取物中分离Pth1抑制化合物可以大大加快传统的生物活性分离,减少时间和费用。该方法一般适用于来自其他细菌物种的pth1,并为推进和加速针对这一有前途的抗菌靶点的抑制剂开发开辟了途径。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Expedited isolation of natural product peptidyl-tRNA hydrolase inhibitors from a Pth1 affinity column.

Expedited isolation of natural product peptidyl-tRNA hydrolase inhibitors from a Pth1 affinity column.

Expedited isolation of natural product peptidyl-tRNA hydrolase inhibitors from a Pth1 affinity column.

New antibiotics and new antibiotic targets are needed to counter the development of bacterial drug resistance that threatens to return the human population to the pre-antibiotic era. Bacterial peptidyl-tRNA hydrolase (Pth1) is a promising new antibiotic target in the early stages of development. While inhibitory activity has been observed in a variety of natural products, bioactive fractionation has been a bottleneck for inhibitor isolation. To expedite the isolation of inhibitory compounds from complex mixtures, we constructed a Pth1 affinity column and used it to isolate inhibitory compounds from crude natural products. Recombinantly produced S. typhimurium Pth1 was covalently attached to a column matrix and the inhibitory activity isolated from ethanol extracts of Salvinia minima. The procedure reported here demonstrates that isolation of Pth1 inhibitory compounds from complex natural product extracts can be greatly expedited over traditional bioactive fractionation, decreasing time and expense. The approach is generally applicable to Pth1s from other bacterial species and opens an avenue to advance and accelerate inhibitor development against this promising antimicrobial target.

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来源期刊
AIMS Molecular Science
AIMS Molecular Science BIOCHEMISTRY & MOLECULAR BIOLOGY-
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