People for and against direct-to-consumer (DTC) genomic tests are arguing around two issues: first, on whether an autonomy-based account can justify the tests; second, on whether the tests bring any personal utility. Bunnik et al, in an article published in this journal, were doubtful on the latter, especially in clinically irrelevant and uninterpretable sequences, and how far this claim could go in the justification. Here we argue that personal utility is inherent to DTC genomic tests and their results. We discuss Bunnik et al's account of personal utility and identify problems in its motivation and application. We then explore concepts like utility and entertainment which suggest that DTC genomic tests bring personal utility to their consumers, both in the motivation and the content of the tests. This points to an alternative account of personal utility which entails that entertainment value alone is adequate to justify DTC genomic tests, given appropriate strategies to communicate tests results with the consumers. It supports the autonomy-based justification of the test by showing that DTC genomic test itself stands as a valuable option and facilitates meaningful choice of the people.

Both soluble Aβ oligomers and insoluble Aβ fibrils are neurotoxic. The former is a better correlate of cognitive dysfunction; Aβ oligomers block long-term potentiation in hippocampal neurons (Tomic, Pensalfini, Head & Glabe, 2009). In Aβ fibrils, β-strands of individual Aβ peptides aggregate to form cross-β structures with inter-strand hydrogen bonds (Figure 1A). This provides surfaces onto which Aβ peptides are favourably "docked-and-locked" (Karran et al., 2011). Therefore, it is intuitive for therapeutics to attempt preventing Aβ aggregates, in both oligomer and fibril states. To design these therapeutic interventions, we need to thoroughly understand the nucleating step, stability, and reversibility of these aggregates. While techniques like NMR contributed greatly to studying the structure of Aβ fibrils, Aβ oligomer structure is less clear due to its heterogeneity, instability, and variability across experimental conditions (Cerasoli, Ryadnov & Austen, 2015) (Figure 1B). The dynamic process of how Aβ is transiently misfolded, aggregates into oligomers, and subsequently forms protofibrils and fibrils is still elusive, due to the limitations of conventional biophysical techniques. In this review, we compare newer spectrometry and spectroscopy techniques with conventional biophysical approaches used in studying Aβ aggregation. In addition, computational strategies like MD simulation have generated insights into the dynamic properties of Aβ aggregates. We discuss their principles and usages and outline how a combination of experimental and computational methods contributes profound insights into Aβ aggregation. Both approaches should go hand in hand in order to understand, not only Aβ but critical peptides and proteins in human diseases.