Relationship between copper(II) complexes with FomA adhesin fragments of F. nucleatum and colorectal cancer. Coordination pattern and ability to promote ROS production

作者: M. K. Lesiów , U. K. Komarnicka , K. Stokowa-Sołtys , K. Rolka , A. Łęgowska

DOI: 10.1039/C7DT04103A

关键词: StereochemistryIon bindingImidazoleRadicalMetal ions in aqueous solutionAscorbic acidChemistryFusobacterium nucleatumCopperGel electrophoresis

摘要: The copper(II) ion binding of the Ac-KGHGNG-NH2 and Ac-PTVHNE-NH2 fragments FomA adhesin from Fusobacterium nucleatum was studied using potentiometry, UV-Vis, CD, EPR DFT techniques. coordination pattern described in a wide range pH values. Ligands begin interactions with metal ions imidazole nitrogen. At 6.8 (a value typical large intestine environment), coordinated by 3N donor atoms {Nim, 2 × N−amide} both cases. However, bound more effectively peptide. formation reactive oxygen species (ROS) UV-Vis fluorescence spectroscopy, as well gel electrophoresis presence H2O2 and/or ascorbic acid. complexes generated ROS highest amounts among all compounds. Moreover, they stimulated CT26 cell line (mouse colon carcinoma) to produce which lead oxidative stress. It also determined that such radicals took part plasmid degradation mechanism.

参考文章(84)
Joshi Pc, Copper(II) as an efficient scavenger of singlet molecular oxygen. Indian Journal of Biochemistry & Biophysics. ,vol. 35, pp. 208- 215 ,(1998)
Kamila Stokowa-Sołtys, Aleksandra Kasprowicz, Jan Wrzesiński, Jerzy Ciesiołka, Nicola Gaggelli, Elena Gaggelli, Gianni Valensin, Małgorzata Jeżowska-Bojczuk, Impact of Cu2 + ions on the structure of colistin and cell-free system nucleic acid degradation Journal of Inorganic Biochemistry. ,vol. 151, pp. 67- 74 ,(2015) , 10.1016/J.JINORGBIO.2015.05.011
Agnieszka Kadej, Mariola Kuczer, Teresa Kowalik-Jankowska, Copper(II) complexes of terminally free alloferon mutants containing two histidyl binding sites inside peptide chain structure and stability Dalton Transactions. ,vol. 44, pp. 20659- 20674 ,(2015) , 10.1039/C5DT01911G
Michael G. Brattain, Janna Strobel-Stevens, Awni M. Sarrif, Maryla Webb, David Fine, Establishment of Mouse Colonic Carcinoma Cell Lines with Different Metastatic Properties Cancer Research. ,vol. 40, pp. 2142- 2146 ,(1980)
Pål Puntervoll, Morten Ruud, Live J. Bruseth, Hans Kleivdal, Bente T. Høgh, Roland Benz, Harald B. Jensen, Structural characterization of the fusobacterial non-specific porin FomA suggests a 14-stranded topology, unlike the classical porins. Microbiology. ,vol. 148, pp. 3395- 3403 ,(2002) , 10.1099/00221287-148-11-3395
Teresa Kowalik-Jankowska, Monika Ruta-Dolejsz, Kornelia Wiśniewska, Leszek Łankiewicz, Coordination of copper(II) ions by the 11–20 and 11–28 fragments of human and mouse β-amyloid peptide Journal of Inorganic Biochemistry. ,vol. 92, pp. 1- 10 ,(2002) , 10.1016/S0162-0134(02)00495-6
John Cunninghamn, Marlene Leffell, Patricia Mearkle, Paul Harmatz, Elevated plasma ceruloplasmin in insulin-dependent diabetes mellitus: Evidence for increased oxidative stress as a variable complication Metabolism-clinical and Experimental. ,vol. 44, pp. 996- 999 ,(1995) , 10.1016/0026-0495(95)90095-0
Klaudia Jomova, Marian Valko, Advances in metal-induced oxidative stress and human disease Toxicology. ,vol. 283, pp. 65- 87 ,(2011) , 10.1016/J.TOX.2011.03.001
Janet Y. Uriu-Adams, Carl L. Keen, Copper, oxidative stress, and human health Molecular Aspects of Medicine. ,vol. 26, pp. 268- 298 ,(2005) , 10.1016/J.MAM.2005.07.015