{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,20]],"date-time":"2025-10-20T00:24:06Z","timestamp":1760919846815,"version":"build-2065373602"},"reference-count":47,"publisher":"Wiley","issue":"24","license":[{"start":{"date-parts":[[2019,11,12]],"date-time":"2019-11-12T00:00:00Z","timestamp":1573516800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["J of Separation Science"],"published-print":{"date-parts":[[2019,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The interactive behavior of an amphipathic peptide with the Cu<jats:sup>2+<\/jats:sup>, Ni<jats:sup>2+<\/jats:sup>, and Zn<jats:sup>2+<\/jats:sup> complexes of 1,4\u2010<jats:italic>bis<\/jats:italic>(triazacyclonon\u20101\u2010yl)butane), <jats:italic>bis<\/jats:italic>(tacn)<jats:sup>but<\/jats:sup>, immobilized onto Sepharose CL\u20104B, has been investigated. The effects of incubation time, as well as the incubation buffer pH and ionic strength, have been examined. The binding data have been interrogated using Langmuir, Langmuir\u2010Freundlich, bi\u2010Langmuir, and Temkin isothermal models and Scatchard plots. These results confirm that this amphipathic peptide binds with relatively high capacities to the immobilized Cu<jats:sup>2+<\/jats:sup>\u2010 and Ni<jats:sup>2+<\/jats:sup>\u20101,4\u2010<jats:italic>bis<\/jats:italic>(triazacyclonon\u20101\u2010yl)butane)\u2010Sepharose CL\u20104B sorbents via at least two discrete sites. However, the corresponding immobilized Zn<jats:sup>2+<\/jats:sup>\u2010sorbent had low binding capacity. Moreover, the magnitude of the binding capacities of these sorbents was dependent on the pH and ionic strength of the incubation buffer. These results are relevant to the isolation of <jats:italic>E. coli<\/jats:italic> expressed recombinant proteins that incorporate this and related amphipathic peptide tags, containing two or more histidine residues, located at the N\u2010 or C\u2010terminus of the recombinant protein, and the co\u2010purification of low abundance host cell proteins of diverse structure, by immobilized metal ion affinity chromatographic methods.<\/jats:p>","DOI":"10.1002\/jssc.201900908","type":"journal-article","created":{"date-parts":[[2019,10,25]],"date-time":"2019-10-25T06:59:11Z","timestamp":1571986751000},"page":"3631-3639","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Interactions between an amphipathic di\u2010histidine peptide and a metal affinity chromatographic resin derived from a <i>bis<\/i>(tacn)butane chelating ligand"],"prefix":"10.1002","volume":"42","author":[{"given":"Ute","family":"Kreher","sequence":"first","affiliation":[{"name":"Centre for Green Chemistry School of Chemistry Monash University  Clayton Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Leone","family":"Spiccia","sequence":"additional","affiliation":[{"name":"Centre for Green Chemistry School of Chemistry Monash University  Clayton Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2744-6531","authenticated-orcid":false,"given":"Milton T. 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