The Role of Copper (II) on Kininogen Binding to Tropomyosin in the Presence of a Histidine–Proline-Rich Peptide
| Autor: | Antonio Magrì, Anna Santoro, Diego La Mendola, Stefania Zimbone, Giulia Grasso |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Kininogen binding histidine–proline-rich glycoprotein Circular dichroism Stereochemistry Metal ions in aqueous solution chemistry.chemical_element kininogen Peptide Zinc 010402 general chemistry 01 natural sciences Catalysis Article Inorganic Chemistry tropomyosin lcsh:Chemistry 03 medical and health sciences angiogenesis Humans histidine– Physical and Theoretical Chemistry Angiogenesis Copper Histidine–proline-rich glycoprotein Kininogen Tropomyosin Molecular Biology lcsh:QH301-705.5 Spectroscopy Histidine proline-rich glycoprotein chemistry.chemical_classification Binding Sites Kininogens Organic Chemistry zinc Proteins General Medicine 0104 chemical sciences Computer Science Applications circular dichroism 030104 developmental biology chemistry lcsh:Biology (General) lcsh:QD1-999 copper Oligopeptides Protein Binding |
| Zdroj: | International Journal of Molecular Sciences, Vol 21, Iss 9343, p 9343 (2020) International Journal of Molecular Sciences Volume 21 Issue 24 International journal of molecular sciences 21 (2020). doi:10.3390/ijms21249343 info:cnr-pdr/source/autori:Santoro, Anna Maria; Zimbone, Stefania; Magri, Antonio; La Mendola, Diego; Grasso, Giulia/titolo:The Role of Copper (II) on Kininogen Binding to Tropomyosin in the Presence of a Histidine-Proline-Rich Peptide/doi:10.3390%2Fijms21249343/rivista:International journal of molecular sciences (Print)/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume:21 |
| ISSN: | 1661-6596 1422-0067 |
| DOI: | 10.3390/ijms21249343 |
| Popis: | The antiangiogenic activity of the H/P domain of histidine&ndash proline-rich glycoprotein is mediated by its binding with tropomyosin, a protein exposed on endothelial cell-surface during the angiogenic switch, in presence of zinc ions. Although it is known that copper ion serum concentration is significantly increased in cancer patients, its role in the interaction of H/P domain with tropomyosin, has not yet been studied. In this paper, by using ELISA assay, we determined the modulating effect of TetraHPRG peptide, a sequence of 20 aa belonging to H/P domain, on the binding of Kininogen (HKa) with tropomyosin, both in absence and presence of copper and zinc ions. A potentiometric study was carried out to characterize the binding mode adopted by metal ions with TetraHPRG, showing the formation of complex species involving imidazole amide nitrogen atoms in metal binding. Moreover, circular dichroism showed a conformational modification of ternary systems formed by TetraHPRG, HKa and copper or zinc. Interestingly, slight pH variation influenced the HKa-TetraHPRG-tropomyosin binding. All these results indicate that both metal ions are crucial in the interaction between TetraHPRG, tropomyosin and HKa. |
| Databáze: | OpenAIRE |
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