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含氮和氧供体配体的配合物作为潜在的脲酶抑制剂

Complexes of N- and O-Donor Ligands as Potential Urease Inhibitors.

作者信息

Shah Syed Raza, Shah Zarbad, Khiat Mohammed, Khan Ajmal, Hill Leila R, Khan Shakeel, Hussain Javid, Csuk René, Anwar Muhammad U, Al-Harrasi Ahmed

机构信息

Natural and Medical Sciences Research Centre, University of Nizwa, Birkat Almouz, Nizwa 616, Oman.

Department of Chemistry, Bacha Khan University Charsadda, Charsadda 24420 Khyber Pakhtunkhwa, Pakistan.

出版信息

ACS Omega. 2020 Apr 20;5(17):10200-10206. doi: 10.1021/acsomega.0c01089. eCollection 2020 May 5.

DOI:10.1021/acsomega.0c01089
PMID:32391508
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7203987/
Abstract

We report five new transition-metal complexes that inhibit the urease enzyme. Barbituric acid (), thiobarbituric acid (), isoniazid (), and nicotinamide () ligands were employed in complexation reactions. The resulting complexes were characterized using a variety of analytical techniques including infra-red and UV-vis spectroscopy, H NMR spectroscopy, elemental analysis, and single-crystal X-ray diffraction analysis. We describe two mononuclear complexes with a general formula {M()(HO)(HO)}, where M = Co () and Zn (), a mononuclear complex {Ni()(HO)(HO)} (), and two polymeric chains of a general formula {M() (HO)(HO)}, where M = Co () and Zn (). These complexes displayed significant urease enzyme inhibition with IC values in the range of 3.9-19.9 μM.

摘要

我们报道了五种抑制脲酶的新型过渡金属配合物。在络合反应中使用了巴比妥酸（）、硫代巴比妥酸（）、异烟肼（）和烟酰胺（）配体。使用包括红外和紫外可见光谱、核磁共振光谱、元素分析和单晶X射线衍射分析在内的多种分析技术对所得配合物进行了表征。我们描述了两种通式为{M()(HO)(HO)}的单核配合物，其中M = Co（）和Zn（），一种单核配合物{Ni()(HO)(HO)}（），以及两种通式为{M() (HO)(HO)}的聚合物链，其中M = Co（）和Zn（）。这些配合物表现出显著的脲酶抑制作用，IC值在3.9 - 19.9 μM范围内。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/47970d324553/ao0c01089_0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/ff7681d31f3e/ao0c01089_0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/e890c31bded7/ao0c01089_0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/5bb1daffa0ea/ao0c01089_0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/ce25e38279da/ao0c01089_0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/a007bcbd7e68/ao0c01089_0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/4fb54cca2d6e/ao0c01089_0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/47970d324553/ao0c01089_0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/ff7681d31f3e/ao0c01089_0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/e890c31bded7/ao0c01089_0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/5bb1daffa0ea/ao0c01089_0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/ce25e38279da/ao0c01089_0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/a007bcbd7e68/ao0c01089_0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/4fb54cca2d6e/ao0c01089_0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61cc/7203987/47970d324553/ao0c01089_0007.jpg

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