دورية أكاديمية
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Macrocyclic peptides as allosteric inhibitors of nicotinamide N -methyltransferase (NNMT).

التفاصيل البيبلوغرافية
العنوان: Macrocyclic peptides as allosteric inhibitors of nicotinamide N -methyltransferase (NNMT).
المؤلفون: van Haren MJ; Biological Chemistry Group, Institute of Biology Leiden, Leiden University Sylviusweg 72 2333 BE Leiden The Netherlands n.i.martin@biology.leidenuniv.nl., Zhang Y; Biological Chemistry Group, Institute of Biology Leiden, Leiden University Sylviusweg 72 2333 BE Leiden The Netherlands n.i.martin@biology.leidenuniv.nl., Thijssen V; Chemical Biology & Drug Discovery Group, Utrecht Institute for Pharmaceutical Sciences Universiteitsweg 99 3584 CG Utrecht The Netherlands s.a.k.jongkees@vu.nl., Buijs N; Biological Chemistry Group, Institute of Biology Leiden, Leiden University Sylviusweg 72 2333 BE Leiden The Netherlands n.i.martin@biology.leidenuniv.nl., Gao Y; Biological Chemistry Group, Institute of Biology Leiden, Leiden University Sylviusweg 72 2333 BE Leiden The Netherlands n.i.martin@biology.leidenuniv.nl., Mateuszuk L; Jagiellonian University, Jagiellonian Centre for Experimental Therapeutics (JCET) Bobrzynskiego 14 30-348 Krakow Poland., Fedak FA; Jagiellonian University, Jagiellonian Centre for Experimental Therapeutics (JCET) Bobrzynskiego 14 30-348 Krakow Poland., Kij A; Jagiellonian University, Jagiellonian Centre for Experimental Therapeutics (JCET) Bobrzynskiego 14 30-348 Krakow Poland., Campagna R; Department of Clinical Sciences, Universitá Politecnica delle Marche Via Ranieri 65 60131 Ancona Italy., Sartini D; Department of Clinical Sciences, Universitá Politecnica delle Marche Via Ranieri 65 60131 Ancona Italy., Emanuelli M; Department of Clinical Sciences, Universitá Politecnica delle Marche Via Ranieri 65 60131 Ancona Italy., Chlopicki S; Jagiellonian University, Jagiellonian Centre for Experimental Therapeutics (JCET) Bobrzynskiego 14 30-348 Krakow Poland.; Jagiellonian University Medical College, Chair of Pharmacology Grzegorzecka 16 31-531 Krakow Poland., Jongkees SAK; Chemical Biology & Drug Discovery Group, Utrecht Institute for Pharmaceutical Sciences Universiteitsweg 99 3584 CG Utrecht The Netherlands s.a.k.jongkees@vu.nl.; Department of Chemistry and Pharmaceutical Sciences, Vrije Universiteit Amsterdam De Boelelaan 1108 1081 HZ Amsterdam The Netherlands., Martin NI; Biological Chemistry Group, Institute of Biology Leiden, Leiden University Sylviusweg 72 2333 BE Leiden The Netherlands n.i.martin@biology.leidenuniv.nl.
المصدر: RSC chemical biology [RSC Chem Biol] 2021 Aug 19; Vol. 2 (5), pp. 1546-1555. Date of Electronic Publication: 2021 Aug 19 (Print Publication: 2021).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Royal Society of Chemistry Country of Publication: England NLM ID: 101768727 Publication Model: eCollection Cited Medium: Internet ISSN: 2633-0679 (Electronic) Linking ISSN: 26330679 NLM ISO Abbreviation: RSC Chem Biol Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Cambridge : Royal Society of Chemistry, [2020]-
مستخلص: Nicotinamide N -methyltransferase (NNMT) methylates nicotinamide to form 1-methylnicotinamide (MNA) using S -adenosyl-l-methionine (SAM) as the methyl donor. The complexity of the role of NNMT in healthy and disease states is slowly being elucidated and provides an indication that NNMT may be an interesting therapeutic target for a variety of diseases including cancer, diabetes, and obesity. Most inhibitors of NNMT described to date are structurally related to one or both of its substrates. In the search for structurally diverse NNMT inhibitors, an mRNA display screening technique was used to identify macrocyclic peptides which bind to NNMT. Several of the cyclic peptides identified in this manner show potent inhibition of NNMT with IC 50 values as low as 229 nM. The peptides were also found to downregulate MNA production in cellular assays. Interestingly, substrate competition experiments reveal that these cyclic peptide inhibitors are noncompetitive with either SAM or NA indicating they may be the first allosteric inhibitors reported for NNMT.
Competing Interests: There are no conflicts to declare.
(This journal is © The Royal Society of Chemistry.)
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تواريخ الأحداث: Date Created: 20211027 Latest Revision: 20211028
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC8496086
DOI: 10.1039/d1cb00134e
PMID: 34704059
قاعدة البيانات: MEDLINE
الوصف
تدمد:2633-0679
DOI:10.1039/d1cb00134e