Buscar

 

RI UFLA (Universidade Federal de Lavras) >
DQI - Departamento de Química >
DQI - Artigos publicados em periódicos >

Por favor, utilize esse identificador para citar este item ou usar como link: http://repositorio.ufla.br/jspui/handle/1/13329

Título: Interaction of chemically modified tetracyclines with catalytic Zn(II) ion in matrix metalloproteinase: evidence for metal coordination sites
Autor(es): Marcial, Bruna L.
Costa, Luiz Antônio S.
Almeid, Wagner B. de
Anconi, Cleber P. A.
Santos, Hélio F. dos
Assunto: Tetracycline
DFT calculations
Matrix metalloproteinase
Chemically modified tetracycline
Tetraciclina
Cálculos DFT
Metalloproteinase de matriz
Tetraciclina modificada quimicamente
Publicador: Springer
Data de publicação: Fev-2011
Referência: MARCIAL, B. L. et al. Interaction of chemically modified tetracyclines with catalytic Zn(II) ion in matrix metalloproteinase: evidence for metal coordination sites. Theoretical Chemistry Accounts, Berlin, v. 128, n. 3, p. 377-388, Feb. 2011.
Abstract: Chemically modified tetracyclines (CMTs) have shown promising activity as matrix metalloproteinase (MMP) inhibitors acting as zinc-binding groups. The first step in the design of new and effective drugs is the molecular description of the mechanism of action in chemical and biological environments. In the present study, the structure and stability of [Zn(LHn)(H2O)2]2−x (n = 0, 1, 2 and x = −2, −1, 0) and [Zn(L)(His)3], where L represents five distinct, structurally related CMTs, are discussed. In addition to the effect of the ligand on Zn(II) coordination, the role of the solvent and pH was also determined. The results suggested that O1–Oam (labeled as site II in the present paper) of CMT-1, CMT-4 and CMT-7 was the most stable site in the gas phase and aqueous solution. However, for CMT-3 and CMT-8, coordination at the O11–O12 moiety (site VI) was preferred. This coordination site is an essential binding mode of CMTs with active zinc in the MMP catalytic site; therefore, our results support the singular behavior of CMT-3 and CMT-8 as promising MMP inhibitors.
URI: https://link.springer.com/article/10.1007/s00214-010-0881-9
http://repositorio.ufla.br/jspui/handle/1/13329
Idioma: en_US
Aparece nas coleções: DQI - Artigos publicados em periódicos

Arquivos neste Item:

Não há arquivos associados para este Item.

Itens protegidos por copyright, com todos os direitos reservados, Salvo indicação em contrário.


Mostrar estatísticas

 


DSpace Software Copyright © 2002-2007 MIT and Hewlett-Packard - Feedback