ABSTRACT
Human islet amyloid polypeptide (hIAPP), or amylin, is a pancreatic hormone and the main constituent of amyloid deposits in type-2 diabetes mellitus (TTDM). The pathological characteristics of TTDM include progressive beta (β)-cell dysfunction, loss of β-cell mass, and formation of toxic amylin oligomers and ibrils or islet amyloidosis. In this chapter, we describe several routinely and less commonly used methods and approaches such as spectroscopy and highresolution scanning microscopy to investigate amylin aggregation in vitro and in situ. We also discuss how combination of atomic force microscopy (AFM), confocal microscopy, and luorescence/CD spectroscopy can be utilized in coherent fashion to examine amylin aggregation, traficking, and toxicity at nm-resolution and in real
Saurabh Trikha, Sanghamitra Singh, and Aleksandar M. Jeremic
time. These technological advancements provide a novel insight into formation and pro-apoptotic action of toxic amylin oligomers and aggregates, knowledge which is critical for the development of novel therapeutics for the treatment of TTDM.
