Transition-metal coordination modulates predicted DNA groove recognition and nucleobase contacts in oligohistidine complexes
Özet
Histidine-rich peptides are widely used in affinity-based purification because imidazole donors can coordinate transition-metal ions. To examine how fixed metal-coordination models may alter the predicted DNA-contacting behavior of a histidine hexamer, a fully in silico comparison was performed using metal-free His6 and the tri-metal model complexes [Zn3(His6)]6+, [Ni3(His6)]6+, and [Cu3(His6)]6+ against the canonical B-DNA dodecamer 1BNA [d(CGCGAATTCGCG)]. The formulas denote the neutral-terminal/neutral-imidazole computational representation used for docking and molecular dynamics (MD), rather than a claim concerning the dominant solution-phase species. Molecular docking and MD simulations were used to compare predicted groove localization, recurrent nucleobase-associated contacts, hydrogen-bond patterns, relative docking scores, and trajectory-based structural persistence. Within the examined 1BNA model, metal-free His6 produced a dominant major-groove pose with adenine-associated contacts and a Vina docking score of −8.9 kcal/mol. The tri-metal coordination models produced dominant minor-groove poses with guanine-associated contacts, with relative docking scores of −9.5, −13.5, and −10.8 kcal/mol for the Zn(II), Ni(II), and Cu(II) models, respectively. The Ni(II)- and Cu(II)-containing models also displayed lower RMSD levels than the metal-free complex over the sampled trajectories. These observations are restricted to the defined computational models and the 1BNA sequence; they do not establish experimental binding affinities, universal nucleobase selectivity, or solution-phase metal speciation. The work provides a hypothesis-generating comparison that may guide future experimental investigation of metal-coordinated oligohistidine-DNA interactions.
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Tam Kayıt
| Alan | Değer | Dil |
|---|---|---|
| dc.contributor.author | Agar, Soykan | |
| dc.contributor.author | Yildiz, Alparslan Numan | |
| dc.contributor.author | Yurtsever, Mine | |
| dc.date.accessioned | 2026-10-27T23:47:32.555413996Z | |
| dc.date.available | 2026-10-27T23:47:32.555413996Z | |
| dc.date.issued | 2026 | |
| dc.description.abstract | Histidine-rich peptides are widely used in affinity-based purification because imidazole donors can coordinate transition-metal ions. To examine how fixed metal-coordination models may alter the predicted DNA-contacting behavior of a histidine hexamer, a fully in silico comparison was performed using metal-free His6 and the tri-metal model complexes [Zn3(His6)]6+, [Ni3(His6)]6+, and [Cu3(His6)]6+ against the canonical B-DNA dodecamer 1BNA [d(CGCGAATTCGCG)]. The formulas denote the neutral-terminal/neutral-imidazole computational representation used for docking and molecular dynamics (MD), rather than a claim concerning the dominant solution-phase species. Molecular docking and MD simulations were used to compare predicted groove localization, recurrent nucleobase-associated contacts, hydrogen-bond patterns, relative docking scores, and trajectory-based structural persistence. Within the examined 1BNA model, metal-free His6 produced a dominant major-groove pose with adenine-associated contacts and a Vina docking score of −8.9 kcal/mol. The tri-metal coordination models produced dominant minor-groove poses with guanine-associated contacts, with relative docking scores of −9.5, −13.5, and −10.8 kcal/mol for the Zn(II), Ni(II), and Cu(II) models, respectively. The Ni(II)- and Cu(II)-containing models also displayed lower RMSD levels than the metal-free complex over the sampled trajectories. These observations are restricted to the defined computational models and the 1BNA sequence; they do not establish experimental binding affinities, universal nucleobase selectivity, or solution-phase metal speciation. The work provides a hypothesis-generating comparison that may guide future experimental investigation of metal-coordinated oligohistidine-DNA interactions. | |
| dc.description.sponsorship | Bilimsel Araştırma Projeleri Birimi, İstanbul Teknik Üniversitesi, BAP, (THD-2024-46299) | |
| dc.description.sponsorship | Sheikh Bahaei National High Performance Computing Center, Isfahan University of Technology, SBNHPCC, (5004452017) | |
| dc.identifier.doi | 10.1080/07391102.2026.2723209 | |
| dc.identifier.eissn | 1538-0254 | |
| dc.identifier.issn | 0739-1102 | |
| dc.identifier.pmid | 42647108 | |
| dc.identifier.scopus | 2-s2.0-105048680028 | |
| dc.identifier.uri | https://rdlopen.rawdatalibrary.net/r/kostu/10445 | |
| dc.identifier.wos | WOS:001861027500001 | |
| dc.language.iso | en | |
| dc.publisher | Taylor and Francis Ltd. | |
| dc.relation.ispartof | Journal of Biomolecular Structure and Dynamics | |
| dc.rights | info:eu-repo/semantics/closedAccess | |
| dc.subject | DNA binding | |
| dc.subject | metal-DNA complexes | |
| dc.subject | molecular docking | |
| dc.subject | molecular dynamics | |
| dc.subject | nucleobase contacts | |
| dc.subject | Oligohistidine | |
| dc.subject.classification | Biochemistry & Molecular Biology | |
| dc.subject.classification | Biophysics | |
| dc.subject.other | RESISTANT ESCHERICHIA-COLI | |
| dc.subject.other | MICROARRAY | |
| dc.subject.other | IDENTIFICATION | |
| dc.subject.other | PURIFICATION | |
| dc.subject.other | VALIDATION | |
| dc.subject.other | DIAGNOSIS | |
| dc.subject.other | ARRAY | |
| dc.title | Transition-metal coordination modulates predicted DNA groove recognition and nucleobase contacts in oligohistidine complexes | |
| dc.type | Article | |
| rdl.citation.openalex | 0 | |
| rdl.citation.scopus | 0 | |
| rdl.citation.wos | 0 | |
| rdl.department | Faculty of Dentistry, Department of Biochemistry, Kocaeli Health and Technology University, Kocaeli, Türkiye | |
| rdl.department | Department of Chemistry, Faculty of Arts and Sciences, Istanbul Technical University, Maslak, Istanbul, Türkiye | |
| rdl.department | Department of Software Engineering, Faculty of Engineering and Architecture, Altınbaş University, Istanbul, Türkiye | |
| rdl.oa.status | closed | |
| rdl.publication.status | inPress | |
| rdl.scopus.quartile | Q2 | |
| rdl.source.index | SCOPUS | |
| rdl.source.index | WOS | |
| rdl.source.index | PUBMED | |
| rdl.wos.index | Science Citation Index Expanded (SCI-EXPANDED) |
