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Amorphous Aggregation of Amyloid Beta 1‐40 Peptide in Confined Space |
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| Authors: | Dr. Giulia Foschi Dr. Cristiano Albonetti Dr. Fabiola Liscio Dr. Silvia Milita Dr. Pierpaolo Greco Prof. Fabio Biscarini |
| Affiliation: | 1. Scriba Nanotecnologie S. r. L., Bologna, Italy;2. Istituto per lo Studio dei Materiali Nanostrutturati - ISMN, Consiglio Nazionale delle Ricerche - CNR, Bologna, Italy);3. Istituto di Microelettronica e Microsistemi - IMM, Consiglio Nazionale delle Ricerche - CNR, Bologna, Italy;4. Dipartimento di Scienze della Vita, Università degli Studi di Modena e Reggio Emilia, Modena, Italy |
| Abstract: | The amorphous aggregation of Aβ1‐40 peptide is addressed by using micromolding in capillaries. Both the morphology and the size of the aggregates are modulated by changing the contact angle of the sub‐micrometric channel walls. Upon decreasing the hydrophilicity of the channels, the aggregates change their morphology from small aligned drops to discontinuous lines, thereby keeping their amorphous structure. Aβ1‐40 fibrils are observed at high contact angles. |
| Keywords: | Alzheimer's disease amyloid biotechnology nanotechnology scanning probe microscopy |