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Zn(II) and Cd(II) complexes of AMT1/MAC1 homologous Cys/His-Rich domains : so similar yet so different
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Rola, Anna, Potok, Paulina, Mos, Magdalena, Gumienna-Kontecka, Elżbieta and Potocki, Sławomir (2022) Zn(II) and Cd(II) complexes of AMT1/MAC1 homologous Cys/His-Rich domains : so similar yet so different. Inorganic Chemistry, 61 (36). pp. 14333-14343. doi:10.1021/acs.inorgchem.2c02080 ISSN 0020-1669.
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WRAP-ZnII-and-CdII-complexes-of-AMT1MAC1-homologous-CysHis-Rich-domains-so-similar-yet-so-different-Mos-2022.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (5Mb) | Preview |
Official URL: http://dx.doi.org/10.1021/acs.inorgchem.2c02080
Abstract
Infections caused by Candida species are becoming seriously dangerous and difficult to cure due to their sophisticated mechanisms of resistance. The host organism defends itself from the invader, e.g., by increasing the concentration of metal ions. Therefore, there is a need to understand the overall mechanisms of metal homeostasis in Candida species. One of them is associated with AMT1, an important virulence factor derived from Candida glabrata, and another with MAC1, present in Candida albicans. Both of the proteins possess a homologous Cys/His-rich domain. In our studies, we have chosen two model peptides, L680 (Ac-10ACMECVRGHRSSSCKHHE27-NH2, MAC1, Candida albicans) and L681 (Ac-10ACDSCIKSHKAAQCEHNDR28-NH2, AMT1, Candida glabrata), to analyze and compare the properties of their complexes with Zn(II) and Cd(II). We studied the stoichiometry, thermodynamic stability, and spectroscopic parameters of the complexes in a wide pH range. When competing for the metal ion in the equimolar mixture of two ligands and Cd(II)/Zn(II), L680 forms more stable complexes with Cd(II) while L681 forms more stable complexes with Zn(II) in a wide pH range. Interestingly, a Glu residue was responsible for the additional stability of Cd(II)-L680. Despite a number of scientific reports suggesting Cd(II) as an efficient surrogate of Zn(II), we showed significant differences between the Zn(II) and Cd(II) complexes of the studied peptides.
Item Type: | Journal Article | ||||||
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Subjects: | Q Science > QD Chemistry Q Science > QK Botany Q Science > QP Physiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Engineering > WMG (Formerly the Warwick Manufacturing Group) | ||||||
Library of Congress Subject Headings (LCSH): | Candida , Candida -- Effect of metals on, Homeostasis, Metal ions, Metal ions -- Absorption and adsorption | ||||||
Journal or Publication Title: | Inorganic Chemistry | ||||||
Publisher: | American Chemical Society | ||||||
ISSN: | 0020-1669 | ||||||
Official Date: | 12 September 2022 | ||||||
Dates: |
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Volume: | 61 | ||||||
Number: | 36 | ||||||
Page Range: | pp. 14333-14343 | ||||||
DOI: | 10.1021/acs.inorgchem.2c02080 | ||||||
Status: | Peer Reviewed | ||||||
Publication Status: | Published | ||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||
Date of first compliant deposit: | 13 September 2022 | ||||||
Date of first compliant Open Access: | 14 September 2022 | ||||||
RIOXX Funder/Project Grant: |
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