当前位置: X-MOL 学术J. Organomet. Chem. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
The synthesis of novel piperazine-benzodioxole substituted phthalocyanines and investigation of their α-amylase and tyrosinase inhibition properties
Journal of Organometallic Chemistry ( IF 2.1 ) Pub Date : 2021-08-01 , DOI: 10.1016/j.jorganchem.2021.122012
İsmail Değirmencioğlu 1 , Fulya Oz Tuncay 1 , Ummuhan Cakmak 1 , Yakup Kolcuoglu 1
Affiliation  

In this study, novel 1-(benzo[d][1,3]dioxol-5-ylmethyl)piperazine substituted phthalocyanine Zn(II), Pb(II) and Co(II) complexes (ZnPc, PbPc, CoPc) were synthesized and proposed structures were confirmed by FT-IR, NMR, UV–vis and MS instrumental techniques. The inhibition potentials of these newly synthesized Pc compounds on, α-amylase and tyrosinase enzymes were investigated. PbPc molecule was found to be most active against α-amylase (IC50 value 7.3 ± 0.3 µM) and tyrosinase (IC50 value 6.7 ± 0.6 µM). Kinetic studies showed that the inhibition mechanism of PbPc molecule on tyrosinase and α-amylase activity was mixed-type.



中文翻译:

新型哌嗪-苯并二氧杂环戊烯取代酞菁的合成及其对α-淀粉酶和酪氨酸酶抑制特性的研究

在这项研究中,新的1-(苯并[ d ] [1,3]二氧杂环戊烯-5-基甲基)哌嗪取代的酞菁锌(II),铅(II)和Co(II)络合物(的ZnPc,PBPC,酞菁钴)合成并通过 FT-IR、NMR、UV-vis 和 MS 仪器技术确认了所提出的结构。研究了这些新合成的Pc化合物对 α-淀粉酶和酪氨酸酶的抑制潜力。发现PbPc分子对 α-淀粉酶(IC 50值 7.3 ± 0.3 µM)和酪氨酸酶(IC 50值 6.7 ± 0.6 µM)最有活性。动力学研究表明PbPc分子对酪氨酸酶和α-淀粉酶活性的抑制机制是混合型的。

更新日期:2021-08-09
down
wechat
bug