دورية أكاديمية
أعرض في EDS

Iron Chelator Transmetalative Approach to Inhibit Human Ribonucleotide Reductase.

التفاصيل البيبلوغرافية
العنوان: Iron Chelator Transmetalative Approach to Inhibit Human Ribonucleotide Reductase.
المؤلفون: Gaur K; Department of Chemistry, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Pérez Otero SC; Department of Chemistry, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Benjamín-Rivera JA; Department of Chemistry, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Rodríguez I; Department of Chemistry, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Loza-Rosas SA; Department of Chemistry, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Vázquez Salgado AM; Department of Biology, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Akam EA; Department of Chemistry and Biochemistry, The University of Arizona, 1306 E. University Blvd., Tucson, Arizona 85721-0041, United States., Hernández-Matias L; Department of Biology, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Sharma RK; Department of Chemistry, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Alicea N; Department of Chemistry, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Kowaleff M; Department of Chemistry, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Washington AV; Department of Biology, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States., Astashkin AV; Department of Chemistry and Biochemistry, The University of Arizona, 1306 E. University Blvd., Tucson, Arizona 85721-0041, United States., Tomat E; Department of Chemistry and Biochemistry, The University of Arizona, 1306 E. University Blvd., Tucson, Arizona 85721-0041, United States., Tinoco AD; Department of Chemistry, University of Puerto Rico Río Piedras Campus, San Juan, Puerto Rico 00931, United States.
المصدر: JACS Au [JACS Au] 2021 Jun 28; Vol. 1 (6), pp. 865-878. Date of Electronic Publication: 2021 May 25.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101775714 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2691-3704 (Electronic) Linking ISSN: 26913704 NLM ISO Abbreviation: JACS Au Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Chemical Society, [2021]-
مستخلص: Efforts directed at curtailing the bioavailability of intracellular iron could lead to the development of broad-spectrum anticancer drugs given the metal's role in cancer proliferation and metastasis. Human ribonucleotide reductase (RNR), the key enzyme responsible for synthesizing the building blocks of DNA replication and repair, depends on Fe binding at its R2 subunit to activate the catalytic R1 subunit. This work explores an intracellular iron chelator transmetalative approach to inhibit RNR using the titanium(IV) chemical transferrin mimetic (cTfm) compounds Ti(HBED) and Ti(Deferasirox) 2 . Whole-cell EPR studies reveal that the compounds can effectively attenuate RNR activity though seemingly causing different changes to the labile iron pool that may account for differences in their potency against cells. Studies of Ti(IV) interactions with the adenosine nucleotide family at pH 7.4 reveal strong metal binding and extensive phosphate hydrolysis, which suggest the capacity of the metal to disturb the nucleotide substrate pool of the RNR enzyme. By decreasing intracellular Fe bioavailability and altering the nucleotide substrate pool, the Ti cTfm compounds could inhibit the activity of the R1 and R2 subunits of RNR. The compounds arrest the cell cycle in the S phase, indicating suppressed DNA replication, and induce apoptotic cell death. Cotreatment cell viability studies with cisplatin and Ti(Deferasirox) 2 reveal a promising synergism between the compounds that is likely owed to their distinct but complementary effect on DNA replication.
Competing Interests: The authors declare no competing financial interest.
(© 2021 The Authors. Published by American Chemical Society.)
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معلومات مُعتمدة: R01 GM127646 United States GM NIGMS NIH HHS; P20 GM103475 United States GM NIGMS NIH HHS; T34 GM007821 United States GM NIGMS NIH HHS; P30 ES006694 United States ES NIEHS NIH HHS; R01 HL090933 United States HL NHLBI NIH HHS; R25 GM061151 United States GM NIGMS NIH HHS; SC1 CA190504 United States CA NCI NIH HHS
تواريخ الأحداث: Date Created: 20210709 Latest Revision: 20240403
رمز التحديث: 20240403
مُعرف محوري في PubMed: PMC8243325
DOI: 10.1021/jacsau.1c00078
PMID: 34240081
قاعدة البيانات: MEDLINE
الوصف
تدمد:2691-3704
DOI:10.1021/jacsau.1c00078