In our effort to develop new synthetic strategies for the isolation of new phosphonate frameworks, we exploited the possibility of simultaneously utilizing benzene‐1,3,5‐triphosphonic acid (H6btp) and di‐2‐pyridyl ketone (py2CO), which is a ma...
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https://www.riss.kr/link?id=O119034279
2018년
-
1434-1948
1099-0682
SCI;SCIE;SCOPUS
학술저널
91-98 [※수록면이 p5 이하이면, Review, Columns, Editor's Note, Abstract 등일 경우가 있습니다.]
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
In our effort to develop new synthetic strategies for the isolation of new phosphonate frameworks, we exploited the possibility of simultaneously utilizing benzene‐1,3,5‐triphosphonic acid (H6btp) and di‐2‐pyridyl ketone (py2CO), which is a ma...
In our effort to develop new synthetic strategies for the isolation of new phosphonate frameworks, we exploited the possibility of simultaneously utilizing benzene‐1,3,5‐triphosphonic acid (H6btp) and di‐2‐pyridyl ketone (py2CO), which is a major player in the field of polynuclear metal complexes. This ligand blend in CuII chemistry afforded a 2D framework comprising tetranuclear [CuII4] secondary building units. A thorough investigation of the CuII/di‐2‐pyridyl ketone/benzene‐1,3,5‐triphosphonic acid reaction system also revealed a hydrogen‐bonded framework. The structure of the latter comprises the cationic [Cu{py2C(OH)2}2]2+ complex [py2C(OH)2 is the hydrate of py2CO], the dianion of benzene‐1,3,5‐triphosphonic acid (H4btp2–) and water solvates. The magnetic properties of the coordination polymer were rationalized on the basis of magnetically isolated [CuII4] units dominated by antiferromagnetic interactions.
The simultaneous use of the metal‐nucleating ligand di‐2‐pyridyl ketone and the bridging benzene‐1,3,5‐triphosphonic acid ligand in CuII chemistry afforded a hydrogen‐bonded framework and a 2D coordination polymer comprising tetranuclear SBUs. The magnetic properties of the product were rationalized on the basis of magnetically isolated [CuII4] units dominated by antiferromagnetic interactions.
CuII Binding to Various Forms of Amyloid‐β Peptides: Are They Friends or Foes?