{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T00:20:08Z","timestamp":1790295608887,"version":"4.1.0"},"reference-count":59,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2023,5,9]],"date-time":"2023-05-09T00:00:00Z","timestamp":1683590400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004281","name":"National Science Center","doi-asserted-by":"publisher","award":["UMO2017\/26\/A\/ST5\/00363"],"award-info":[{"award-number":["UMO2017\/26\/A\/ST5\/00363"]}],"id":[{"id":"10.13039\/501100004281","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004281","name":"National Science Center","doi-asserted-by":"publisher","award":["UMO2017\/26\/E\/ST5\/00364"],"award-info":[{"award-number":["UMO2017\/26\/E\/ST5\/00364"]}],"id":[{"id":"10.13039\/501100004281","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004281","name":"National Science Center","doi-asserted-by":"publisher","award":["UMO-2021\/41\/B\/ST4\/02654"],"award-info":[{"award-number":["UMO-2021\/41\/B\/ST4\/02654"]}],"id":[{"id":"10.13039\/501100004281","id-type":"DOI","asserted-by":"publisher"}]},{"name":"European Cooperation in Science and Technology","award":["UMO2017\/26\/A\/ST5\/00363"],"award-info":[{"award-number":["UMO2017\/26\/A\/ST5\/00363"]}]},{"name":"European Cooperation in Science and Technology","award":["UMO2017\/26\/E\/ST5\/00364"],"award-info":[{"award-number":["UMO2017\/26\/E\/ST5\/00364"]}]},{"name":"European Cooperation in Science and Technology","award":["UMO-2021\/41\/B\/ST4\/02654"],"award-info":[{"award-number":["UMO-2021\/41\/B\/ST4\/02654"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Histidine and cysteine residues, with their imidazole and thiol moieties that deprotonate at approximately physiological pH values, are primary binding sites for Zn(II), Ni(II) and Fe(II) ions and are thus ubiquitous both in peptidic metallophores and in antimicrobial peptides that may use nutritional immunity as a way to limit pathogenicity during infection. We focus on metal complex solution equilibria of model sequences encompassing Cys\u2013His and His\u2013Cys motifs, showing that the position of histidine and cysteine residues in the sequence has a crucial impact on its coordination properties. CH and HC motifs occur as many as 411 times in the antimicrobial peptide database, while similar CC and HH regions are found 348 and 94 times, respectively. Complex stabilities increase in the series Fe(II) &lt; Ni(II) &lt; Zn(II), with Zn(II) complexes dominating at physiological pH, and Ni(II) ones\u2014above pH 9. The stabilities of Zn(II) complexes with Ac-ACHA-NH2 and Ac-AHCA-NH2 are comparable, and a similar tendency is observed for Fe(II), while in the case of Ni(II), the order of Cys and His does matter\u2014complexes in which the metal is anchored on the third Cys (Ac-AHCA-NH2) are thermodynamically stronger than those where Cys is in position two (Ac-ACHA-NH2) at basic pH, at which point amides start to take part in the binding. Cysteine residues are much better Zn(II)-anchoring sites than histidines; Zn(II) clearly prefers the Cys\u2013Cys type of ligands to Cys\u2013His and His\u2013Cys ones. In the case of His- and Cys-containing peptides, non-binding residues may have an impact on the stability of Ni(II) complexes, most likely protecting the central Ni(II) atom from interacting with solvent molecules.<\/jats:p>","DOI":"10.3390\/molecules28103985","type":"journal-article","created":{"date-parts":[[2023,5,10]],"date-time":"2023-05-10T01:57:51Z","timestamp":1683683871000},"page":"3985","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["CH vs. HC\u2014Promiscuous Metal Sponges in Antimicrobial Peptides and Metallophores"],"prefix":"10.3390","volume":"28","author":[{"given":"Kinga","family":"Garstka","sequence":"first","affiliation":[{"name":"Faculty of Chemistry, University of Wroc\u0142aw, F. Joliot-Curie 14, 50-383 Wroc\u0142aw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valentyn","family":"Dzyhovskyi","sequence":"additional","affiliation":[{"name":"Faculty of Chemistry, University of Wroc\u0142aw, F. Joliot-Curie 14, 50-383 Wroc\u0142aw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joanna","family":"W\u0105t\u0142y","sequence":"additional","affiliation":[{"name":"Faculty of Chemistry, University of Wroc\u0142aw, F. Joliot-Curie 14, 50-383 Wroc\u0142aw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4723-0658","authenticated-orcid":false,"given":"Kamila","family":"Stokowa-So\u0142tys","sequence":"additional","affiliation":[{"name":"Faculty of Chemistry, University of Wroc\u0142aw, F. Joliot-Curie 14, 50-383 Wroc\u0142aw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jolanta","family":"\u015awi\u0105tek-Koz\u0142owska","sequence":"additional","affiliation":[{"name":"Faculty of Health Sciences, University of Opole, 68 Katowicka St., 45-060 Opole, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Henryk","family":"Koz\u0142owski","sequence":"additional","affiliation":[{"name":"Faculty of Chemistry, University of Wroc\u0142aw, F. Joliot-Curie 14, 50-383 Wroc\u0142aw, Poland"},{"name":"Faculty of Health Sciences, University of Opole, 68 Katowicka St., 45-060 Opole, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4309-4118","authenticated-orcid":false,"given":"Miquel","family":"Barcel\u00f3-Oliver","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Balearic Islands, Cra. de Valldemossa, km 7.5., 07122 Palma de Mallorca, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2634-0228","authenticated-orcid":false,"given":"Denise","family":"Bellotti","sequence":"additional","affiliation":[{"name":"Faculty of Chemistry, University of Wroc\u0142aw, F. Joliot-Curie 14, 50-383 Wroc\u0142aw, Poland"},{"name":"Department of Chemical, Pharmaceutical and Agricultural Sciences, University of Ferrara, I-44121 Ferrara, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magdalena","family":"Rowi\u0144ska-\u017byrek","sequence":"additional","affiliation":[{"name":"Faculty of Chemistry, University of Wroc\u0142aw, F. Joliot-Curie 14, 50-383 Wroc\u0142aw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,5,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"D1087","DOI":"10.1093\/nar\/gkv1278","article-title":"APD3: The antimicrobial peptide database as a tool for research and education","volume":"44","author":"Wang","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"6217","DOI":"10.1039\/C9DT01015G","article-title":"The ability of the NiSOD binding loop to chelate zinc(II): The role of the terminal amino group in the enzymatic functions","volume":"48","author":"Csire","year":"2019","journal-title":"Dalton Trans."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1038\/s41579-022-00745-6","article-title":"Nutritional immunity: The battle for nutrient metals at the host\u2013pathogen interface","volume":"20","author":"Murdoch","year":"2022","journal-title":"Nat. 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