Table 2. Secreted destruxins in the ex vivo culturing system.

[M+H]+	RT/min	R	AA2	AA3	AA4	AA5	AA6	destruxin	fold change on brain	fold change on muscle
564.3392	11.53	CH = CH2	Pro	Val	mVal	mAla	Ala	A2	D 9.7
564.3392	10.92	CH = CH2	Pro	Lxx	Val	mAla	Ala	DesmA	L 5.4
566.3392	11.64	CH-(CH3)2	Pro	Val	Val	mAla	Ala	this study
578.3548	11.7	CH = CH2	Pro	Lxx	mVal	mAla	Ala	A	D 24.7
580.3340	9.34	CH(O)CH2	Pro	Lxx	Val	mAla	Ala	this study	D 128.3
580.3704	12.22	CH-(CH3)2	Pro	Val	mVal	mAla	Ala	B2	D 13.5
580.3704	12.5	CH-(CH3)2	Pro	Lxx	Val	mAla	Ala	DesmB	D 9.0
594.3861	12.73	CH-(CH3)2	Pro	Lxx	mVal	mAla	Ala	B	D 36.2	L 23.1
594.3497	10.17	CH(O)CH2	Pro	Lxx	mVal	mAla	Ala	E
596.3654	9.55	COH-(CH3)2	Pro	Lxx	Val	mAla	Ala	DesmC
610.3810	10.39	COH-(CH3)2	Pro	Lxx	mVal	mAla	Ala	C	D 16.3
610.3446	9.53	CH2-CH2COOH	Pro	Lxx	Val	mAla	Ala	this study
612.3603	8.69	CH2OH-CH2OH	Pro	Lxx	mVal	mAla	Ala	Ed
624.3603	10.34	CH2-CH2COOH	Pro	Lxx	mVal	mAla	Ala	D

For each identified destruxin the accurate mass of the protonated molecular ion, retention time, R and the identities of the amino acids in positions 2–6 are given (Figure 4b). The ones discovered in other studies are indicated by the letter assigned to them. The fold changes found for the majority of them on brain and muscle indicate the tissue specificity of these destruxins. Most of them are heterogeneously secreted on dead tissues (indicated by D), while two are secreted on live tissue (indicated by L). The destruxin mentioned in gray was identified in our raw data set but not of enough abundance to be used in the further analysis of the data.