π‐System Functionalization Transforms Amyloidogenic Peptide Fragment of Human Islet Amyloid Polypeptide into a Super Hydrogelator
| Autor: | Anagha C. Unnikrishnan, Abinaya Sushana Thennarasu, Puchalapalli Saveri, Suryalakshmi Pandurangan, Abhijit P. Deshpande, Niraikulam Ayyadurai, Ganesh Shanmugam |
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| Rok vydání: | 2023 |
| Předmět: | |
| Zdroj: | Chemistry – An Asian Journal. 18 |
| ISSN: | 1861-471X 1861-4728 |
| DOI: | 10.1002/asia.202201235 |
| Popis: | While a considerable number of ultra-short/short amyloid peptides have been reported to form 3D supramolecular hydrogels, they all possess high minimum gelation concentration(MGC)(≥1wt%), which preclude their applications. In this context, we demonstrate that functionalisation of a well-known amyloidogenic ultra-short peptide fragment NFGAIL(IAPf) of human Islet amyloid polypeptide with a π-system (Fluorenyl, Fm) at the N-terminus of the peptide(Fm-IAPf) yield not only highly thermostable hydrogel at physiological pH but also exhibited super gelator nature as the MGC(0.08wt%) falls below 0.1wt%. Various experimental results confirmed that aromatic π-π interactions from fluorenyl moieties and hydrogen bonding interactions between the IAPf drive the self-assembly/fibril formation. Fm-IAPf is the first super hydrogelator derived from amyloid-based ultra-short peptides, to the best of our knowledge. We strongly believe that this report, i.e., functionalization of an amyloid peptide with π-system, provides a lead to develop super hydrogelators from other amyloid-forming peptide fragments for their potential applications. |
| Databáze: | OpenAIRE |
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