Investigations of copper(II) complexation by fragments of the FBP28 protein using isothermal titration (ITC) and differential scanning calorimetry (DSC)

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• 作者：Joanna Makowska ; Dariusz Wyrzykowski…
• 关键词：FBP28 protein fragments ; Metal–peptide binding ; ITC ; DSC
• 刊名：Journal of Thermal Analysis and Calorimetry
• 出版年：2015
• 出版时间：July 2015
• 年：2015
• 卷：121
• 期：1
• 页码：263-268
• 全文大小：679 KB
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• 作者单位：Joanna Makowska (1)
  Dariusz Wyrzykowski (1)
  Paulina Hirniak (1)
  Dorota Uber (1)
  Lech Chmurzyński (1)
  
  1. Faculty of Chemistry, University of Gdańsk, ul. Wita Stwosza 63, 80-308, Gdańsk, Poland
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Sciences
  Polymer Sciences
  Physical Chemistry
  Inorganic Chemistry
  Measurement Science and Instrumentation
  
• 出版者：Akad茅miai Kiad贸, co-published with Springer Science+Business Media B.V., Formerly Kluwer Academic
• ISSN：1572-8943

文摘

Isothermal titration calorimetry (ITC) was used to study the interactions between copper(II) ions and peptides with sequences taken from the N-terminal loop of the FBP28 protein (formin-binding protein) WW domain: Ac-Lys-Thr-Ala-Asp-Gly-Lys-Thr-NH2 (D7) and Ac-Tyr-Lys-Thr-Ala-Asn-Gly-Lys-Thr-Tyr-NH2 (D9?M), respectively. Measurements were taken at 298.15?K in 20?mM 2-(N-morpholino)ethanesulfonic acid buffer solution at a pH of 6. The stoichiometry, conditional stability constants and thermodynamic parameters (ΔITC G, ΔITC H and ΔITC S) for the pertinent complexation reactions were determined. Furthermore, the thermal stability of peptide conformations in the presence and absence of copper(II) in the system was investigated using differential scanning calorimetry. Finally, a general procedure on how to include the effect of buffer competition with the peptide for the metal as well as proton competition with the metal for the peptide and the buffer’s component during ITC data analysis is described.