Scientific Reports

Table 1 Monitoring fibril formation by thioflavin T (ThT) fluorescence.

From: Identification of key regions and residues controlling Aβ folding and assembly

Peptide	Metric¹	Positions of D-amino acids
Peptide	Metric¹	WT	1,2	3,4	5,6	7,8	10,11	12,13	14,15	16,17	18,19	20,21	22,23	23,24	26,27	27,28	30,31	31,32	34,35	35,36	39,40	41,42
Aβ40	FU _max	196	320	335	180	317	236	1434	130	2900	1773	1657	1616	76	15.7	1344	143	215	1145	348	597	N/A
	t _1/2	219	82	96	70	198	229	290	141	228	148	206	131	226	115	269	262	187	246	296	213	N/A
	dFU/dt	0.86	2.20	1.70	1.21	0.90	0.98	6.97	0.85	10.72	10.46	8.97	27.24	0.34	0.07	9.48	0.48	1.40	5.44	2.96	6.17	N/A
		WT	D3	D4	D16	D17	D26	D27	D28
	FU _max	125	225	192	38	1909	29	28	276
	t _1/2	160	163	117	128	136	115	121	112
	dFU/dt	0.66	1.16	0.95	0.13	11.25	0.12	0.10	2.39
Aβ42		WT	1,2	3,4	5,6	7,8	10,11	12,13	14,15	16,17	18,19	20,21	22,23	23,24	26,27	27,28	30,31	31,32	34,35	35,36	39,40	41,42
	FU _max	132	87	86	88	108	117	48	354	74	113	235	82	127	192	58	108	60	137	364	151	226
	t _1/2	90	103	82	106	88	201	153	229	104	122	190	68	108	247	128	215	133	133	154	162	123
	dFU/dt	0.71	0.44	0.62	0.41	0.67	0.96	0.15	2.64	0.47	0.75	0.61	0.36	0.50	1.35	0.20	0.40	0.19	0.61	2.35	1.02	0.94
		WT	D12	D13	D14	D15	D20	D21	D26	D28	D35	D36
	FU _max	77	76	59	352	58	605	29	123	103	317	123
	t _1/2	45	214	136	172	82	78	107	173	147	133	101
	dFU/dt	0.50	0.32	0.32	0.98	0.33	3.23	0.09	0.31	0.55	1.24	0.78

Wild type, doubly and singly substituted Aβ40 and Aβ42 peptides at concentrations of 40 or 20 μM, respectively, were co-incubated with 120 μM ThT in 10 mM sodium phosphate, pH 7.4, at 37°C with shaking.¹Continuous monitoring of fluorescence was done until plateau fluorescence levels had been reached, after which maximum fluorescence (FU_max; FU), the time at which 1/2 FU_max was observed (t_1/2; h), and the rate of increase in fluorescence (dFU/dt; FU·h⁻¹) were determined. N/A is “not applicable.”

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