Investigations into the Mechanism of Fibril Formation in a Peptide Hydrogel

The mechanism of self-assembly of a hydrogel-forming peptide was investigated, using kinetics assays (which relate the rate of aggregation to underlying physical processes) and disc centrifugation (which reports on the length of the peptide fibrils in the gel). The kinetics assays reveal that aggregation in this system is consistent with a secondary mechanism of fibril formation. These assays also show that the aggregations kinetics are concentration dependent only up to 50 μM, suggesting that one or more processes saturate above this concentration. The disc centrifugation data show an inverse relationship between monomer concentration and fibril length, which could result from the combination of a saturating fibril growth mechanism and a non-saturating fibril formation mechanism. Future directions for this project include seeded kinetics assays (in which pre-formed fibrils are used to accelerate aggregation) and disc centrifugation studies which focus on fibril length as a function of time, both of which would help determine between possible aggregation mechanisms