Table 1.

Circular Dichroism Assay at Different Time Points Shows the Percentages of α-Helix, β-Sheet, and Random Coil as Calculated by the Lincomb and Convex Constraint Algorithms

Time (h)	Aβ1-42			Aβ1-30-NH2			K6-Aβ1-30-NH2
	α-Helix	β-Sheet	Random coil	α-Helix	β-Sheet	Random coil	α-Helix	β-Sheet	Random coil
0	9	36	55	5	37	58	2	18	79
24	9	40	51	8	36	56	5	16	78
96	5	55	40	7	49	44	34	16	50

Both Aβ1–42 and Aβ1–30 had a high β-sheet content that increased throughout time. The peptide with the polylysine at the N-terminus (K6Aβ1–30-NH₂) had a much lower β-sheet content that did not increase with incubation.