Amyloids can have normal biological functions. 1r3 However, amyloidogenic proteins can also form unwanted oligomeric or polymeric aggregates when disturbed from their native functional states. Such aggregates are associated with numerous neurodegenerative diseases, such as diabetes type II, 4 Alzheimer (AD), Parkinson, Huntington, and prion (“mad cow”) diseases, amyotrophic lateral sclerosis, and Down’s syndrome (DS). 5r9 Increasing evidence from studies in human, transgenic mice, cultured cells, wild type rodent, and in vitro systems indicates that soluble oligomers of amyloidogenic proteins are both responsible for amyloidosis10, 11 and are the toxic agent. 12r14 Some data suggest that their final large aggregates can also lead to cytotoxicity. 15, 16 Ordered aggregates can extend into β-strand enriched fibrils, regardless of their initial native conformational states. Experimental and computational approaches revealed structural details of these organizations. Amyloid structural models were obtained by different methods: spectroscopy, 17r23 solid-state NMR (ssNMR), 24r29 EPR, 30, 31 hydrogen/deuterium exchange, 15, 27, 32 cryo-electron microscopy (cryo-EM) and electron microscopy (EM), 33r36 X-ray fiber diffraction and X-ray diffraction, 37r41 and peptide design. 42 Apart from a handful of peptides that were successfully crystallized providing insight into the ordered amyloid arrangement, 43 amyloid structural elucidation has been fraught with difficulties. The insolubility of amyloid fibrils has made crystallization and solution NMR virtually impossible. Under these circumstances, ssNMR has been the method of choice for structural determination, providing insight into the nature of β-sheet organization. 44 ssNMR data of Aβ segments coupled with atomistic molecular dynamic simulations have further been useful in addressing the driving forces for targeted associations. 45, 46