Ile-phe dipeptide self-assembly: clues to amyloid formation |
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Authors: | de Groot Natalia Sánchez Parella Teodor Aviles Francesc X Vendrell Josep Ventura Salvador |
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Institution: | Natalia Sánchez de Groot, Teodor Parella, Francesc X. Aviles, Josep Vendrell, and Salvador Ventura |
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Abstract: | Peptidic self-assembled nanostructures are said to have a wide range of applications in nanotechnology, yet the mechanistic details of hierarchical self-assembly are still poorly understood. The Phe-Phe recognition motif of the Alzheimer's Aβ peptide is the smallest peptide able to assemble into higher-order structures. Here, we show that the Ile-Phe dipeptide analog is also able to self-associate in aqueous solution as a transparent, thermoreversible gel formed by a network of fibrillar nanostructures that exhibit strong birefringence upon Congo red binding. Besides, a second dipeptide Val-Phe, differing only in a methyl group from the former, is unable to self-assemble. The detailed analysis of the differential polymeric behavior of these closely related molecules provides insight into the forces triggering the first steps in self-assembly processes such as amyloid formation. |
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