{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T11:05:22Z","timestamp":1789470322919,"version":"build-2803163510"},"reference-count":57,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T00:00:00Z","timestamp":1784505600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T00:00:00Z","timestamp":1784505600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Biopolymers"],"published-print":{"date-parts":[[2026,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Green fluorescent protein (GFP) was originally obtained from\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Aequorea victoria<\/jats:italic>\n                    <\/jats:styled-content>\n                    and was successfully synthesized through recombinant technology. In this study, we revealed novel, fascinating insights into the properties of this well\u2010known GFP by examining a traditional GFP separation process involving aqueous two\u2010phase systems and several liquid chromatographs. We investigated the impact of organic solvents and salts on the conformation of GFP by measuring its fluorescence intensity and circular dichroism spectrum, and then proposed an optimized process to improve the yield of fluorescent GFP. We have noticed that fluorescent GFP migrates anomalously to ~37\u2009kDa on non\u2010heating SDS\u2010PAGE due to retention of its compact \u03b2\u2010barrel conformation, whereas the commonly reported 27\u2009kDa migration corresponds to the fully heat\u2010denatured, non\u2010fluorescent form. Nevertheless, the most exciting discovery is that the purified GFP exhibited a remarkable ability to self\u2010assemble into an intriguing fluorescent leaf\u2010like structure upon evaporation\u2010concentration under ambient conditions. To our knowledge, this represents the first direct visualization of such macroscopic fluorescent leaf\u2010like assemblies formed by recombinant GFP, with fluorescence retained throughout the assembled morphology. This captivating phenomenon may have promising implications for protein\u2010based nanomaterials and will inspire further exploration of protein self\u2010assembly nanotechnology.\n                  <\/jats:p>","DOI":"10.1002\/bip.70118","type":"journal-article","created":{"date-parts":[[2026,7,21]],"date-time":"2026-07-21T04:17:19Z","timestamp":1784607439000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Fluorescent Leaf\u2010Like Structures Formed by Self\u2010Assembly of Green Fluorescent Protein"],"prefix":"10.1002","volume":"117","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2523-591X","authenticated-orcid":false,"given":"Hsi\u2010Chi","family":"Lu","sequence":"first","affiliation":[{"name":"Department of Food Science Tunghai University  Taichung 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