دورية أكاديمية
أعرض في EDS

Iso-mukaadial acetate and ursolic acid acetate inhibit the chaperone activity of Plasmodium falciparum heat shock protein 70-1.

التفاصيل البيبلوغرافية
العنوان: Iso-mukaadial acetate and ursolic acid acetate inhibit the chaperone activity of Plasmodium falciparum heat shock protein 70-1.
المؤلفون: Salomane N; Department of Biochemistry, Faculty of Science, University of Johannesburg, Johannesburg, 2006, South Africa., Pooe OJ; Discipline of Biochemistry, School of Life Sciences, University of KwaZulu-Natal, Westville, Durban, 4000, South Africa., Simelane MBC; Department of Biochemistry, Faculty of Science, University of Johannesburg, Johannesburg, 2006, South Africa. msimelane@uj.ac.za.
المصدر: Cell stress & chaperones [Cell Stress Chaperones] 2021 Jul; Vol. 26 (4), pp. 685-693. Date of Electronic Publication: 2021 May 23.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 9610925 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1466-1268 (Electronic) Linking ISSN: 13558145 NLM ISO Abbreviation: Cell Stress Chaperones Subsets: MEDLINE
أسماء مطبوعة: Publication: 2024- : [New York] : Elsevier
Original Publication: New York : Churchill Livingstone, c1996-
مواضيع طبية MeSH: HSP70 Heat-Shock Proteins/*drug effects , HSP70 Heat-Shock Proteins/*metabolism , Molecular Chaperones/*metabolism , Plasmodium falciparum/*metabolism , Triterpenes/*pharmacology, Adenosine Triphosphatases/metabolism ; Antimalarials/chemistry ; Antimalarials/metabolism ; Antimalarials/pharmacology ; Escherichia coli/metabolism ; Plasmodium falciparum/drug effects ; Prospective Studies ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Ursolic Acid
مستخلص: Plasmodium falciparum is the most lethal malaria parasite. The present study investigates the interaction capabilities of select plant derivatives, iso-mukaadial acetate (IMA) and ursolic acid acetate (UAA), against P. falciparum Hsp70-1 (PfHsp70-1) using in vitro approaches. PfHsp70-1 facilitates protein folding in the parasite and is deemed a prospective antimalarial drug target. Recombinant PfHsp70-1 protein was expressed in E. coli BL21 cells and homogeneously purified by affinity chromatography. The interaction between the compounds and PfHsp70-1 was evaluated using malate dehydrogenase (MDH), and luciferase aggregation assay, ATPase activity assay, and Fourier transform infrared (FTIR). PfHsp70-1 prevented the heat-induced aggregation of MDH and luciferase. However, the PfHsp70-1 chaperone role was inhibited by IMA or UAA, leading to both MDH and luciferase's thermal aggregation. The basal ATPase activity of PfHsp70-1 (0.121 nmol/min/mg) was closer to UAA (0.131 nmol/min/mg) (p = 0.0675) at 5 mM compound concentration, suggesting that UAA has no effect on PfHsp70-1 ATPase activity. However, ATPase activity inhibition was similar between IMA (0.068 nmol/min/mg) (p < 0.0001) and polymyxin B (0.083 nmol/min/mg) (p < 0.0001). The lesser the Pi values, the lesser ATP hydrolysis observed due to compound binding to the ATPase domain. FTIR spectra analysis of IMA and UAA resulted in PfHsp70-1 structural alteration for β-sheets shifting the amide I band from 1637 cm -1 to 1639 cm -1 , and for α-helix from 1650 cm -1 to 1652 cm -1 , therefore depicting secondary structural changes with an increase in secondary structure percentage suggesting that these compounds interact with PfHsp70-1.
(© 2021. Cell Stress Society International.)
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فهرسة مساهمة: Keywords: Heat shock protein; Iso-mukaadial acetate; Plasmodium falciparum; Polymyxin B; Ursolic acid acetate
المشرفين على المادة: 0 (Antimalarials)
0 (HSP70 Heat-Shock Proteins)
0 (Molecular Chaperones)
0 (Recombinant Proteins)
0 (Triterpenes)
0 (heat-shock protein 70.1)
EC 3.6.1.- (Adenosine Triphosphatases)
تواريخ الأحداث: Date Created: 20210523 Date Completed: 20220125 Latest Revision: 20240209
رمز التحديث: 20240209
مُعرف محوري في PubMed: PMC8275760
DOI: 10.1007/s12192-021-01212-6
PMID: 34023985
قاعدة البيانات: MEDLINE
الوصف
تدمد:1466-1268
DOI:10.1007/s12192-021-01212-6