. 2015 Apr 21;4(1):A0037. doi: 10.5702/massspectrometry.A0037

Table 7. Sensitivity improvement by ATHAP for peptides with SSRCalc Hydrophobicity from 5.2 to 54.8.^a⁾ [Reproduced from ref. 33 with Copyright permission of American Chemical Society.].

Analytes				Sensitivity improvement rate (fold)
No.	Name	SSRCalc Hydrophobicity	m/z (Ave.)	Sensitivity improvement rate (fold)
1	NF-κB inhibitor	54.8	2782.6	10
2	OVA-BIP hybrid peptide	50.2	2291.6	10
3	Humanin	50.0	2688.3	10
4	β-Amyloid 22–42	42.4	2000.4	10
5	Catestatin	38.1	2327.7	1
6	ACTH 18–39	37.9	2466.7	1
7	Nocistatin	29.8	1928.1	1
8	Neuropeptide S	22.3	2188.5	0.1
9	β-Amyloid 1–16	18.2	1956.1	0.1
10	β-Amyloid 1–11	13.5	1326.3	0.001
11	β-Conglycinin 165–178	5.2	1848.8	0.0001

^a⁾ Sensitivity improvement for peptides with SSRCalc Hydrophobicity from 5.2 to 54.8 using ATHAP, compared with CHCA in positive-ion mode. The sensitivity improvement rate was calculated by dividing the detection limit using CHCA by that using ATHAP.

Table 7. Sensitivity improvement by ATHAP for peptides with SSRCalc Hydrophobicity from 5.2 to 54.8.a) [Reproduced from ref. 33 with Copyright permission of American Chemical Society.].

Table 7. Sensitivity improvement by ATHAP for peptides with SSRCalc Hydrophobicity from 5.2 to 54.8.^a⁾ [Reproduced from ref. 33 with Copyright permission of American Chemical Society.].