Aleksandra Hecel-Czaplicka
In 2017, she received her PhD with distinction at the University of Wrocław with a dissertation titled The influence of the structure of the amyloidogenic fragment of human and avian prion protein on its interaction with Cu(II) and Cu(I) ions (supervisor: Prof. Henryk Kozłowski).
From August 2020 to October 2022, she carried out her postdoctoral research at the University of Zurich in the group of Prof. Eva Freisinger, focusing on the role of Cu(I) ions in the properties of newly identified fungal metallothioneins.
Her research interests lie in bioinorganic chemistry of metal-binding and metal-transport systems with particular attention to bacterial metal acquisition (including chalcophores) and proteins involved in metal homeostasis.
Research projects:
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NCN SONATA 19 project Deciphering the diverse bioinorganic chemistry of ‘putative’ bacterial copper-ion transporters (2024–2027),
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NAWA Bekker project Bioinorganic secrets of chalcophores—how microorganisms acquire copper ions
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IDUB internal grant Deciphering the mechanism of chalcophore and copper ion transport by the OprC membrane protein

List of papers:
G. Potoczniak, A. Ślusarczyk, K. Szarszoń, J. Gawłowski, W. Lizak, E. Dzień, H. Kozłowski, K. Garstka-Litwin, M. Dziadas, A. Hecel, et al., “BIOLOGICZNIE AKTYWNE METALOPEPTYDY (BAM): OD HOMEOSTAZY METALI U PATOGENÓW DO PRECYZYJNEGO DOSTRAJANIA AKTYWNOŚCI PEPTYDÓW PRZECIWDROBNOUSTROJOWYCH,” Wiadomości Chemiczne, Feb. 2026.
DOI: https://doi.org/10.53584/WIADCHEM.2026.02.22
K. Garstka, A. Hecel, H. Kozłowski, A. Dominguez-Martin, K. Szewczyk, and M. Rowińska-Żyrek, “AdcA lipoprotein involved in Zn(II) transport in Streptococcus mutans – is it as metal-specific as expected?” Dalton Transactions, 2025. DOI: https://doi.org/10.1039/d5dt00131e
M. Pakowski and A. Hecel, “Two sites, two stories: sequence-driven divergence in Cu(II) and Zn(II) binding to CusF,” Dalton Transactions, 2025. DOI: https://doi.org/10.1039/D5DT01770J
A. Hecel, A. Kola, A. Dominguez-Martin, and D. Valensin, “Small Cysteine-Rich Motif, Big Function─Metal-Driven Dimerization of the CopY C-Terminal Fragment,” Inorganic Chemistry, Nov. 2025. DOI: https://doi.org/10.1021/acs.inorgchem.5c03226
A. Hecel, A. Kola, D. Valensin, and D. Witkowska, “Thiol, His–His Motif, and the Battle over Cu(II) in the Relationship of CopM Metallophore and OprC Outer Membrane Protein,” Inorganic Chemistry, Feb. 2025.
DOI: https://doi.org/10.1021/acs.inorgchem.4c05101
E. Dzień, J. Wątły, A. Hecel, A. Mikołajczyk, A. Matera-Witkiewicz, M. Adrover, M. Barceló-Oliver, A. Domínguez-Martín, and M. Rowińska-Żyrek, “Zn(II) coordination influences the secondary structure, but not antimicrobial activity of the N-terminal histatin 3 hydrolysis product,” Dalton Transactions, 2024. DOI: https://doi.org/10.1039/d4dt02274b
A. Miller, A. Mikołajczyk, D. Bellotti, K. Garstka, J. Wątły, A. Hecel, R. Wieczorek, A. Matera-Witkiewicz, and M. Rowińska-Żyrek, “Zn(II) and Cu(II) Coordination Enhances the Antimicrobial Activity of Piscidin 3, but Not That of Piscidins 1 and 2,” Inorganic Chemistry, Jul. 2024. DOI: https://doi.org/10.1021/acs.inorgchem.4c01659
J. Kamińska, A. Hecel, J. Słowik, A. Rombel-Bryzek, M. Rowińska-Żyrek, and D. Witkowska, “Characterization of four peptides from milk fermented with kombucha cultures and their metal complexes—in search of new biotherapeutics,” Frontiers in Molecular Biosciences, Apr. 2024. DOI: https://doi.org/10.3389/fmolb.2024.1366588
A. Hecel, K. Garstka, H. Kozłowski, and M. Rowińska-Żyrek, “–HH and –HAAAH motifs act as fishing nets for biologically relevant metal ions in metallopeptides,” Journal of Inorganic Biochemistry, Mar. 2024. DOI: https://doi.org/10.1016/j.jinorgbio.2023.112456
H. Kozlowski, K. Piasta, A. Hecel, M. Rowinska-Zyrek, and E. Gumienna-Kontecka, “Metallophores: How do human pathogens withdraw metal ions from the colonized host,” in Book chapter, 2023. DOI: https://doi.org/10.1016/B978-0-12-823144-9.00086-8
D. Bellotti, S. Leveraro, A. Hecel, and M. Remelli, “Investigation of metal interactions with YrpE protein of Bacillus subtilis by a polyhistidine peptide model,” Analytical Biochemistry, Nov. 2023. DOI: https://doi.org/10.1016/j.ab.2023.115315
D. Dudek, A. Miller, A. Hecel, A. Kola, D. Valensin, A. Mikołajczyk, M. Barcelo-Oliver, A. Matera-Witkiewicz, and M. Rowińska-Żyrek, “Semenogelins Armed in Zn(II) and Cu(II): May Bioinorganic Chemistry Help Nature to Cope with Enterococcus faecalis?” Inorganic Chemistry, Aug. 2023. DOI: https://doi.org/10.1021/acs.inorgchem.3c02390
J. Wątły, A. Hecel, R. Wieczorek, M. Rowińska-Żyrek, and H. Kozłowski, “Poly-Gly Region Regulates the Accessibility of Metal Binding Sites in Snake Venom Peptides,” Inorganic Chemistry, Sep. 2022. DOI: https://doi.org/10.1021/acs.inorgchem.2c02584
K. Garstka, A. Hecel, H. Kozłowski, and M. Rowińska-Żyrek, “Specific Zn(II)-binding site in the C-terminus of Aspf2, a zincophore from Aspergillus fumigatus,” Metallomics, Jul. 2022. DOI: https://doi.org/10.1093/mtomcs/mfac042
D. Dudek, K. Garstka, A. Miller, E. Dzień, J. Wątły, A. Hecel, H. Kozłowski, and M. Rowińska-Żyrek, “ODDZIAŁYWANIE PRZECIWDROBNOUSTROJOWYCH PEPTYDÓW Z JONAMI METALI – RELACJA MIĘDZY CHEMIĄ KOORDYNACYJNĄ, STRUKTURĄ, TERMODYNAMIKĄ A SPOSOBEM DZIAŁANIA,” Wiadomości Chemiczne, Jun. 2022.
DOI: https://doi.org/10.53584/wiadchem.2022.5.7
A. Hecel, A. Kola, D. Valensin, H. Kozlowski, and M. Rowinska-Zyrek, “Metal specificity of the Ni(II) and Zn(II) binding sites of the N-terminal and G-domain of E. coli HypB,” Dalton Transactions, 2021. DOI: https://doi.org/10.1039/D1DT02126E
A. Hecel, M. Ostrowska, K. Stokowa-Sołtys, J. Wątły, D. Dudek, A. Miller, S. Potocki, A. Matera-Witkiewicz, A. Dominguez-Martin, H. Kozłowski, et al., “Zinc(II)—The Overlooked Éminence Grise of Chloroquine’s Fight against COVID-19?” Pharmaceuticals, Sep. 2020. DOI: https://doi.org/10.3390/ph13090228
A. Kola, A. Hecel, S. Lamponi, and D. Valensin, “Novel Perspective on Alzheimer’s Disease Treatment: Rosmarinic Acid Molecular Interplay with Copper(II) and Amyloid β,” Life, Jul. 2020. DOI: https://doi.org/10.3390/life10070118
A. Hecel, A. Kola, D. Valensin, H. Kozlowski, and M. Rowinska-Zyrek, “Metal Complexes of Two Specific Regions of ZnuA, a Periplasmic Zinc(II) Transporter from Escherichia coli,” Inorganic Chemistry, Feb. 2020.
DOI: https://doi.org/10.1021/acs.inorgchem.9b03298
S. Ben-Shushan, A. Hecel, M. Rowinska-Zyrek, H. Kozlowski, and Y. Miller, “Zinc Binding Sites Conserved in Short Neuropeptides Containing a Diphenylalanine Motif,” Inorganic Chemistry, Jan. 2020. DOI: https://doi.org/10.1021/acs.inorgchem.9b03199
A. Hecel, P. Kolkowska, K. Krzywoszynska, A. Szebesczyk, M. Rowinska-Zyrek, and H. Kozlowski, “Ag+ complexes as potential therapeutic agents in medicine and pharmacy,” Current Medicinal Chemistry, 2019. DOI: https://doi.org/10.2174/0929867324666170920125943
A. Hecel, D. Valensin, and H. Kozłowski, “How copper ions and membrane environment influence the structure of the human and chicken tandem repeats domain?” Journal of Inorganic Biochemistry, 2019. DOI: https://doi.org/10.1016/j.jinorgbio.2018.11.012
J. Wątły, A. Hecel, R. Wieczorek, J. Świątek-Kozłowska, H. Kozłowski, and M. Rowińska-Żyrek, “Uncapping the N-terminus of a ubiquitous His-tag peptide enhances its Cu2+ binding affinity,” Dalton Transactions, 2019.
DOI: https://doi.org/10.1039/c9dt01635j
G. De Gregorio, F. Biasotto, A. Hecel, M. Luczkowski, H. Kozlowski, and D. Valensin, “Structural analysis of copper(I) interaction with amyloid β peptide,” Journal of Inorganic Biochemistry, Jun. 2019. DOI: https://doi.org/10.1016/j.jinorgbio.2019.03.006
A. Hecel, M. Rowińska-Żyrek, and H. Kozłowski, “Copper(II)-Induced Restructuring of ZnuD, a Zinc(II) Transporter from Neisseria meningitidis,” Inorganic Chemistry, May 2019. DOI: https://doi.org/10.1021/acs.inorgchem.9b00265
A. Hecel, J. Wątły, M. Rowińska-Żyrek, J. Świątek-Kozłowska, and H. Kozłowski, “Histidine tracts in human transcription factors: insight into metal ion coordination ability,” Journal of Biological Inorganic Chemistry, 2018.
DOI: https://doi.org/10.1007/s00775-017-1512-x
J. Wątły, A. Hecel, M. Rowińska-Żyrek, and H. Kozłowski, “Impact of histidine spacing on modified polyhistidine tag – Metal ion interactions,” Inorganica Chimica Acta, 2018. DOI: https://doi.org/10.1016/j.ica.2017.06.053
J. Wątły, A. Hecel, P. Kolkowska, H. Kozlowski, and M. Rowinska-Zyrek, “Poly-Xaa sequences in proteins - Biological role and interactions with metal ions: Chemical and medical aspects,” Current Medicinal Chemistry, 2018.
DOI: https://doi.org/10.2174/0929867324666170428104928
A. Hecel, S. Draghi, D. Valensin, and H. Kozlowski, “The effect of a membrane-mimicking environment on the interactions of Cu2+ with an amyloidogenic fragment of chicken prion protein,” Dalton Transactions, 2017.
DOI: https://doi.org/10.1039/c7dt01069a
P. Kołkowska, A. Hecel, D. Kędzierska, M. Ostrowska, P. K. Walencik, J. Wątły, K. Zdyb, M. Spodzieja, S. Rodziewicz-Motowidlo, S. Potocki, et al., “HENRYK — An endless source of metal coordination surprises,” Journal of Inorganic Biochemistry, 2016.
DOI: https://doi.org/10.1016/j.jinorgbio.2016.02.030
A. Hecel, R. De Ricco, and D. Valensin, “Influence of membrane environments and copper ions on the structural features of amyloidogenic proteins correlated to neurodegeneration,” Coordination Chemistry Reviews, 2016.
DOI: https://doi.org/10.1016/j.ccr.2016.06.018
D. Valensin, E. M. Padula, A. Hecel, M. Luczkowski, and H. Kozlowski, “Specific binding modes of Cu(I) and Ag(I) with neurotoxic domain of the human prion protein,” Journal of Inorganic Biochemistry, 2016. DOI: https://doi.org/10.1016/j.jinorgbio.2015.11.015
A. Perczel, A. G. Atanasov, V. Sklenář, J. Nováček, V. Papoušková, P. Kadeřávek, L. Žídek, H. Kozłowski, J. Wątły, A. Hecel, et al., “The eighth central european conference ‘chemistry towards biology’: Snapshot,” Molecules, 2016.
DOI: https://doi.org/10.3390/molecules21101381
A. Hecel, C. Migliorini, D. Valensin, M. Luczkowski, and H. Kozlowski, “Impact of SDS surfactant on the interactions of Cu(2+) ions with the amyloidogenic region of human prion protein,” Dalton Transactions, 2015. DOI: https://doi.org/10.1039/c5dt01488c
