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Article ; Online: Investigation of metal interactions with YrpE protein of Bacillus subtilis by a polyhistidine peptide model.

Bellotti, Denise / Leveraro, Silvia / Hecel, Aleksandra / Remelli, Maurizio

2023 Volume 680, Page(s) 115315

Abstract: The use of model peptides that can simulate the behaviour of a protein domain is a very successful analytical method to study the metal coordination sites in biological systems. Here we study zinc and copper binding ability of the sequence HTHEHSHDHSHAH, ...

Abstract	The use of model peptides that can simulate the behaviour of a protein domain is a very successful analytical method to study the metal coordination sites in biological systems. Here we study zinc and copper binding ability of the sequence HTHEHSHDHSHAH, which serves as model for the metal interactions with YrpE, a putative metal-binding protein of the ZinT family identified in Bacillus subtilis. Compared to other ZinT proteins secreted by Gram-negative bacteria, the metal-coordination properties of YrpE N-terminal histidine-rich domain have not been yet characterized. Different independent analytical methods, aimed at providing information on the stability and structure of the formed species, have been employed, including potentiometric titrations, electrospray ionization mass spectrometry, UV-Vis spectrophotometry, circular dichroism and electron paramagnetic resonance spectroscopy. The obtained speciation models and equilibrium constants allowed to compare the metal-binding ability of the investigated polyhistidine sequence with that of other well-known histidine-rich peptides. Our thermodynamic results revealed that the YrpE domain HTHEHSHDHSHAH forms more stable metal complexes than other His-rich domains of similar ZinT proteins. Moreover, the studied peptide, containing the alternated (-XH-)
MeSH term(s)	Histidine ; Bacillus subtilis ; Peptides ; Metals ; Zinc
Chemical Substances	polyhistidine (26062-48-6) ; Histidine (4QD397987E) ; Peptides ; Metals ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2023-09-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2023.115315
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Article: Characterization of four peptides from milk fermented with kombucha cultures and their metal complexes-in search of new biotherapeutics.

Kamińska, Justyna / Hecel, Aleksandra / Słowik, Joanna / Rombel-Bryzek, Agnieszka / Rowińska-Żyrek, Magdalena / Witkowska, Danuta

Frontiers in molecular biosciences

2024 Volume 11, Page(s) 1366588

Abstract: The most common skin diseases include eczema, psoriasis, acne, and fungal infections. There is often no effective cure for them. Increasing antimicrobial drug resistance prompts us to search for new, safe, and effective therapeutics. Among such ... ...

Abstract	The most common skin diseases include eczema, psoriasis, acne, and fungal infections. There is often no effective cure for them. Increasing antimicrobial drug resistance prompts us to search for new, safe, and effective therapeutics. Among such interesting candidates are peptides derived from milk fermented with specific lactic acid bacteria or with kombucha cultures, which are a potential treasure trove of bioactive peptides. Four of them are discussed in this article. Their interactions with zinc and copper ions, which are known to improve the well-being of the skin, were characterized by potentiometry, MS, ITC, and spectroscopic methods, and their cytostatic potential was analyzed. The results suggest that they are safe for human cells and can be used alone or in complexes with copper for further testing as potential therapeutics for skin diseases.
Language	English
Publishing date	2024-04-04
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2814330-9
ISSN	2296-889X
ISSN	2296-889X
DOI	10.3389/fmolb.2024.1366588
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Article ; Online: -HH and -HAAAH motifs act as fishing nets for biologically relevant metal ions in metallopeptides.

Hecel, Aleksandra / Garstka, Kinga / Kozłowski, Henryk / Rowińska-Żyrek, Magdalena

Journal of inorganic biochemistry

2023 Volume 252, Page(s) 112456

Abstract: Histidine are one of the most common residues involved in transition metal ion binding in the active sites of metalloenzymes. In order to mimic enzymatic metal binding sites, it is crucial to understand the basic coordination modes of histidine residues, ...

Abstract	Histidine are one of the most common residues involved in transition metal ion binding in the active sites of metalloenzymes. In order to mimic enzymatic metal binding sites, it is crucial to understand the basic coordination modes of histidine residues, distributed at different positions in the peptide sequence. We show that: (i) the separation of two histidines has a large effect on complex stability - a sequence with adjusting histidine residues forms more stable complexes with Zn(II) than the one in which the residues are separated, while the contrary is observed for Cu(II) complexes, in which amide nitrogens participate in metal binding. No pronounced effect is observed for Ni(II) complexes, where the amides participate in binding at higher pH; (ii) non-coordinating amino acid residues (basic, acidic and aromatic ones) have a significant impact on complex stability; charged and aromatic residues may enhance Zn(II) binding, while the contrary is observed for the amide-binding Cu(II); (iii) cysteine containing sequences are much more effective Zn(II) and Ni(II) binding motifs at pH above 8, while histidine containing ligands are more suitable for effective Zn(II) and Ni(II) binding at lower pH.
MeSH term(s)	Amides ; Amino Acid Sequence ; Binding Sites ; Copper/chemistry ; Histidine/chemistry ; Metals/metabolism
Chemical Substances	Amides ; Copper (789U1901C5) ; Histidine (4QD397987E) ; Metals
Language	English
Publishing date	2023-12-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	162843-4
ISSN	1873-3344 ; 0162-0134
ISSN (online)	1873-3344
ISSN	0162-0134
DOI	10.1016/j.jinorgbio.2023.112456
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Article ; Online: Investigation of metal interactions with YrpE protein of Bacillus subtilis by a polyhistidine peptide model

Bellotti, Denise / Leveraro, Silvia / Hecel, Aleksandra / Remelli, Maurizio

Analytical Biochemistry. 2023 Nov., v. 680 p.115315-

2023

Abstract	The use of model peptides that can simulate the behaviour of a protein domain is a very successful analytical method to study the metal coordination sites in biological systems. Here we study zinc and copper binding ability of the sequence HTHEHSHDHSHAH, which serves as model for the metal interactions with YrpE, a putative metal-binding protein of the ZinT family identified in Bacillus subtilis. Compared to other ZinT proteins secreted by Gram-negative bacteria, the metal-coordination properties of YrpE N-terminal histidine-rich domain have not been yet characterized. Different independent analytical methods, aimed at providing information on the stability and structure of the formed species, have been employed, including potentiometric titrations, electrospray ionization mass spectrometry, UV–Vis spectrophotometry, circular dichroism and electron paramagnetic resonance spectroscopy. The obtained speciation models and equilibrium constants allowed to compare the metal-binding ability of the investigated polyhistidine sequence with that of other well-known histidine-rich peptides. Our thermodynamic results revealed that the YrpE domain HTHEHSHDHSHAH forms more stable metal complexes than other His-rich domains of similar ZinT proteins. Moreover, the studied peptide, containing the alternated (-XH-)ₙ motif, proved to be even more effective than the His6-tag (widely used in immobilized metal ion affinity chromatography) in binding zinc ions.
Keywords	Bacillus subtilis ; affinity chromatography ; circular dichroism spectroscopy ; electron paramagnetic resonance spectroscopy ; electrospray ionization mass spectrometry ; models ; peptides ; protein domains ; thermodynamics ; zinc ; Metal-protein interaction ; Peptide models ; Polyhistidine tag ; Analytical methods ; Solution equilibria
Language	English
Dates of publication	2023-11
Publishing place	Elsevier Inc.
Document type	Article ; Online
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2023.115315
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Specific Zn(II)-binding site in the C-terminus of Aspf2, a zincophore from Aspergillus fumigatus.

Garstka, Kinga / Hecel, Aleksandra / Kozłowski, Henryk / Rowińska-Żyrek, Magdalena

Metallomics : integrated biometal science

2022 Volume 14, Issue 7

Abstract: Aspergillus fumigatus, one of the most widespread opportunistic human fungal pathogens, adapts to zinc limitation by secreting a 310 amino acid Aspf2 zincophore, able to specifically bind Zn(II) and deliver it to a transmembrane zinc transporter, ZrfC. ... ...

Abstract	Aspergillus fumigatus, one of the most widespread opportunistic human fungal pathogens, adapts to zinc limitation by secreting a 310 amino acid Aspf2 zincophore, able to specifically bind Zn(II) and deliver it to a transmembrane zinc transporter, ZrfC. In this work, we focus on the thermodynamics of Zn(II) complexes with unstructured regions of Aspf2; basing on a variety of spectrometric and potentiometric data, we show that the C-terminal part has the highest Zn(II)-binding affinity among the potential binding sites, and Ni(II) does not compete with Zn(II) binding to this region. The 14 amino acid Aspf2 C-terminus coordinates Zn(II) via two Cys thiolates and two His imidazoles and it could be considered as a promising A. fumigatus targeting molecule.
MeSH term(s)	Amino Acids ; Aspergillus fumigatus/metabolism ; Binding Sites ; Humans ; Protein Domains ; Zinc/metabolism
Chemical Substances	Amino Acids ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2022-06-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2474317-3
ISSN	1756-591X ; 1756-5901
ISSN (online)	1756-591X
ISSN	1756-5901
DOI	10.1093/mtomcs/mfac042
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Article: Novel Perspective on Alzheimer's Disease Treatment: Rosmarinic Acid Molecular Interplay with Copper(II) and Amyloid β.

Kola, Arian / Hecel, Aleksandra / Lamponi, Stefania / Valensin, Daniela

Life (Basel, Switzerland)

2020 Volume 10, Issue 7

Abstract: Alzheimer's disease is a severe disorder that affects millions of people worldwide. It is a very debilitating disease with no cure at the moment. The necessity of finding an effective treatment is very demanding, and the entire scientific community is ... ...

Abstract	Alzheimer's disease is a severe disorder that affects millions of people worldwide. It is a very debilitating disease with no cure at the moment. The necessity of finding an effective treatment is very demanding, and the entire scientific community is putting in a lot of effort to address this issue. The major hallmark of Alzheimer's disease is the presence of toxic aggregated species in the brain, impaired metal homeostasis, and high levels of oxidative stress. Rosmarinic acid is a well-known potent antioxidant molecule, the efficacy of which has been proved both in vitro and in vivo. In this study, we investigated the possible role played by rosmarinic acid as a mediator of the copper(II)-induced neurotoxicity. Several spectroscopic techniques and biological assays were applied to characterize the metal complexes and to evaluate the cytotoxicity and the mutagenicity of rosmarinic acid and its Cu(II) complex. Our data indicate that rosmarinic acid is able to interfere with the interaction between amyloid β and Cu(II) by forming an original ternary association.
Language	English
Publishing date	2020-07-20
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2662250-6
ISSN	2075-1729
ISSN	2075-1729
DOI	10.3390/life10070118
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Article ; Online: Poly-Gly Region Regulates the Accessibility of Metal Binding Sites in Snake Venom Peptides.

Wa Tły, Joanna / Hecel, Aleksandra / Wieczorek, Robert / Rowińska-Żyrek, Magdalena / Kozłowski, Henryk

Inorganic chemistry

2022 Volume 61, Issue 36, Page(s) 14247–14251

Abstract: It is supposed that the presence of poly-His regions in close proximity to poly-Gly domains in snake venoms is related to their biological activity; poly-His/poly-Gly (pHpG) peptides inhibit the activity of metalloproteinases during venom storage via the ...

Abstract	It is supposed that the presence of poly-His regions in close proximity to poly-Gly domains in snake venoms is related to their biological activity; poly-His/poly-Gly (pHpG) peptides inhibit the activity of metalloproteinases during venom storage via the chelation metal ions, necessary for their proper functioning. This work shows that only the histidyl residues from the N-terminal VDHDHDH motif (but not from the poly-His tag) were the primary Zn(II) binding sites and that the poly-Gly domain situated in the proximity of a central proline residue may play a regulatory role in venom gland protection. The proline induces a kink of the peptide, resulting in steric hindrance, which may modulate the accessibility of potential metal binding sites in the poly-His domain and may, in turn, be one of the regulators of Zn(II) accessibility in the venom gland and therefore a modulator of metalloproteinase activity during venom storage.
MeSH term(s)	Amino Acid Sequence ; Binding Sites ; Peptides/chemistry ; Proline ; Snake Venoms
Chemical Substances	Peptides ; Snake Venoms ; Proline (9DLQ4CIU6V)
Language	English
Publishing date	2022-08-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	1484438-2
ISSN	1520-510X ; 0020-1669
ISSN (online)	1520-510X
ISSN	0020-1669
DOI	10.1021/acs.inorgchem.2c02584
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Article ; Online: Semenogelins Armed in Zn(II) and Cu(II): May Bioinorganic Chemistry Help Nature to Cope with

Dudek, Dorota / Miller, Adriana / Hecel, Aleksandra / Kola, Arian / Valensin, Daniela / Mikołajczyk, Aleksandra / Barcelo-Oliver, Miquel / Matera-Witkiewicz, Agnieszka / Rowińska-Żyrek, Magdalena

Inorganic chemistry

2023 Volume 62, Issue 34, Page(s) 14103–14115

Abstract: Proteolytic degradation of semenogelins, the most abundant proteins from human semen, results in the formation of 26- and 29-amino acid peptides (SgIIA and SgI-29, respectively), which share a common 15 amino acid fragment (Sg-15). All three ligands are ... ...

Abstract	Proteolytic degradation of semenogelins, the most abundant proteins from human semen, results in the formation of 26- and 29-amino acid peptides (SgIIA and SgI-29, respectively), which share a common 15 amino acid fragment (Sg-15). All three ligands are effective Zn(II) and Cu(II) binders; in solution, a variety of differently metalated species exist in equilibrium, with the [NH
MeSH term(s)	Humans ; Enterococcus faecalis ; Copper/chemistry ; Chemistry, Bioinorganic ; Anti-Infective Agents ; Zinc/chemistry
Chemical Substances	Copper (789U1901C5) ; Anti-Infective Agents ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2023-08-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	1484438-2
ISSN	1520-510X ; 0020-1669
ISSN (online)	1520-510X
ISSN	0020-1669
DOI	10.1021/acs.inorgchem.3c02390
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Article ; Online: Copper(II)-Induced Restructuring of ZnuD, a Zinc(II) Transporter from Neisseria meningitidis.

Hecel, Aleksandra / Rowińska-Żyrek, Magdalena / Kozłowski, Henryk

Inorganic chemistry

2019 Volume 58, Issue 9, Page(s) 5932–5942

Abstract: Cluster 2 ( ...

Abstract	Cluster 2 (
MeSH term(s)	Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Cation Transport Proteins/chemistry ; Cation Transport Proteins/metabolism ; Copper/chemistry ; Copper/metabolism ; Humans ; Meningococcal Infections/microbiology ; Models, Molecular ; Neisseria meningitidis/chemistry ; Neisseria meningitidis/metabolism ; Protein Binding ; Thermodynamics ; Zinc/chemistry ; Zinc/metabolism
Chemical Substances	Bacterial Proteins ; Cation Transport Proteins ; ZnuD protein, Neisseria meningitidis ; Copper (789U1901C5) ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2019-04-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	1484438-2
ISSN	1520-510X ; 0020-1669
ISSN (online)	1520-510X
ISSN	0020-1669
DOI	10.1021/acs.inorgchem.9b00265
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Article ; Online: Novel Perspective on Alzheimer’s Disease Treatment

Arian Kola / Aleksandra Hecel / Stefania Lamponi / Daniela Valensin

Life, Vol 10, Iss 118, p

Rosmarinic Acid Molecular Interplay with Copper(II) and Amyloid β

2020 Volume 118

Abstract: Alzheimer’s disease is a severe disorder that affects millions of people worldwide. It is a very debilitating disease with no cure at the moment. The necessity of finding an effective treatment is very demanding, and the entire scientific community is ... ...

Abstract	Alzheimer’s disease is a severe disorder that affects millions of people worldwide. It is a very debilitating disease with no cure at the moment. The necessity of finding an effective treatment is very demanding, and the entire scientific community is putting in a lot of effort to address this issue. The major hallmark of Alzheimer’s disease is the presence of toxic aggregated species in the brain, impaired metal homeostasis, and high levels of oxidative stress. Rosmarinic acid is a well-known potent antioxidant molecule, the efficacy of which has been proved both in vitro and in vivo. In this study, we investigated the possible role played by rosmarinic acid as a mediator of the copper(II)-induced neurotoxicity. Several spectroscopic techniques and biological assays were applied to characterize the metal complexes and to evaluate the cytotoxicity and the mutagenicity of rosmarinic acid and its Cu(II) complex. Our data indicate that rosmarinic acid is able to interfere with the interaction between amyloid β and Cu(II) by forming an original ternary association.
Keywords	amyloid β ; copper ; rosmarinic acid ; antioxidant ; polyphenols ; Science ; Q
Language	English
Publishing date	2020-07-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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