Interest in the phenomenon of amyloid formation by peptides and proteins has developed with extraordinary rapidity in recent years, such that is now a major topic of research across a wide range of disciplines. The reasons for this surge of interest arise primarily from the links between amyloid formation and a range of rapidly proliferating medical disorders such as Alzheimer’s disease and type-2 diabetes, and also from the insights that studies of the amyloid state can provide about the nature of the biologically functional forms of peptides and proteins and the means of the maintenance of protein homeostasis within healthy living systems. Recent progress in understanding the factors affecting the stability of the amyloid state relative to that of the native state of a protein, along with the development of methods for defining the mechanism of the conversion between the different states, has led to a much more detailed understanding of the links between protein aggregation, amyloid formation and human disease. This talk will give an overview of recent advances in this field of study and discuss recent progress from our own laboratory towards understanding the structural and physical properties of the amyloid state, the kinetics and mechanism of its formation, and the nature and origins of its links with disease. In addition, the talk will discuss the ways in which protein aggregation and amyloid formation may be inhibited or suppressed, both to understand the nature of protein homeostasis in naturally functioning organisms and also to address the development of therapeutic strategies through which to combat the loss of homeostasis and the onset and progression of disease.