{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T05:03:19Z","timestamp":1790139799103,"version":"4.0.1"},"reference-count":141,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T00:00:00Z","timestamp":1790035200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T00:00:00Z","timestamp":1790035200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100002301","name":"Eesti Teadusagentuur","doi-asserted-by":"publisher","award":["PRG3076"],"award-info":[{"award-number":["PRG3076"]}],"id":[{"id":"10.13039\/501100002301","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100013281","name":"Joint Programming Initiative on Antimicrobial Resistance","doi-asserted-by":"publisher","award":["MOB3ERA1"],"award-info":[{"award-number":["MOB3ERA1"]}],"id":[{"id":"10.13039\/100013281","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["430578458"],"award-info":[{"award-number":["430578458"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000921","name":"European Cooperation in Science and Technology","doi-asserted-by":"publisher","award":["CA23111"],"award-info":[{"award-number":["CA23111"]}],"id":[{"id":"10.13039\/501100000921","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Chemistry A European J"],"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>Self\u2010assembly of DNA, peptides, and proteins provides inherently unique yet essential functionality in biological systems. The inimitable specific binding interaction of DNA, as well as the spontaneous transition of peptide or protein molecules into highly organized superstructures, can be harnessed for sophisticated artificial materials and nanostructure fabrication. Because of their unprecedented programmability and addressability, DNA nanostructures and especially DNA origami nanostructures provide a modular platform for the development of hybrid DNA\u2010peptide and DNA\u2010protein systems. In this Perspective, we discuss how DNA nanostructures can be leveraged to control peptide and protein self\u2010assembly, thus enabling the creation of new and increasingly sophisticated hybrid biomaterials, the single\u2010molecule study of peptide\u2013peptide self\u2010assembly, and the development of therapeutic tools to modulate disease\u2010related amyloid aggregation. Additionally, coiled coil motifs, as an example, can be used as programmable building blocks in DNA nanotechnology for the peptide and protein\u2010mediated hierarchical self\u2010assembly of DNA nanostructures. Finally, we address the potential of DNA nanostructure\u2010templated protein self\u2010assembly. This Perspective highlights current challenges, emerging applications, and future opportunities that are shaping this rapidly growing research area at the interface between nanotechnology, supramolecular chemistry, biomolecular engineering, and biomedicine.<\/jats:p>","DOI":"10.1002\/chem.71726","type":"journal-article","created":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T04:17:36Z","timestamp":1790137056000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["DNA Nanotechnology Meets Peptide and Protein Self\u2010Assembly"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5024-1684","authenticated-orcid":false,"given":"Marcel","family":"Hanke","sequence":"first","affiliation":[{"name":"Technical and Macromolecular Chemistry Paderborn University  Paderborn Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-0409-5737","authenticated-orcid":false,"given":"Nanjundan","family":"Raghul","sequence":"additional","affiliation":[{"name":"Faculty of Chemistry Bielefeld University  Bielefeld Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7139-3110","authenticated-orcid":false,"given":"Adrian","family":"Keller","sequence":"additional","affiliation":[{"name":"Technical and Macromolecular Chemistry Paderborn University  Paderborn Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2762-1555","authenticated-orcid":false,"given":"Veikko","family":"Linko","sequence":"additional","affiliation":[{"name":"Institute of Technology University of Tartu  Tartu Estonia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7937-1880","authenticated-orcid":false,"given":"Ver\u00f3nica I.","family":"Dodero","sequence":"additional","affiliation":[{"name":"Faculty of Chemistry Bielefeld University  Bielefeld Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,22]]},"reference":[{"issue":"5564","key":"e_1_2_11_2_1","doi-asserted-by":"crossref","first-page":"2418","DOI":"10.1126\/science.1070821","article-title":"Self\u2010Assembly at All Scales","volume":"295","author":"Whitesides G. 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