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In this context, we demonstrate that functionalisation of a well\u2010known amyloidogenic ultra\u2010short peptide fragment NFGAIL (IAPf) of human Islet amyloid polypeptide with a \u03c0\u2010system (Fluorenyl, Fm) at the N\u2010terminus of the peptide (Fm\u2010IAPf) yield not only highly thermostable hydrogel at physiological pH but also exhibited super gelator nature as the MGC (0.08\u2005wt%) falls below 0.1\u2005wt%. Various experimental results confirmed that aromatic \u03c0\u2013\u03c0 interactions from fluorenyl moieties and hydrogen bonding interactions between the IAPf drive the self\u2010assembly\/fibril formation. Fm\u2010IAPf is the first super hydrogelator derived from amyloid\u2010based ultra\u2010short peptides, to the best of our knowledge. We strongly believe that this report, i.\u2009e., functionalization of an amyloid peptide with \u03c0\u2010system, provides a lead to develop super hydrogelators from other amyloid\u2010forming peptide fragments for their potential applications.<\/jats:p>","DOI":"10.1002\/asia.202201235","type":"journal-article","created":{"date-parts":[[2022,12,25]],"date-time":"2022-12-25T22:02:09Z","timestamp":1672005729000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["\u03c0\u2010System Functionalization Transforms Amyloidogenic Peptide Fragment of Human Islet Amyloid Polypeptide into a Super Hydrogelator"],"prefix":"10.1002","volume":"18","author":[{"given":"Anagha C.","family":"Unnikrishnan","sequence":"first","affiliation":[{"name":"Organic &amp; Bioorganic Chemistry Laboratory Council of Scientific and Industrial Research (CSIR) \u2013 Central Leather Research Institute (CLRI)  Adyar 600020 Chennai 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