Table 1 Summary of disulfide-constrained peptides produced in AC-assisted Ec CFS.

Name	^aN/C	Spacer	^bGSH/ time	^cRGS- removal	^dAssay	POI-RGS ^e(μM)	Figure ^fSN
SFTI	prm	GAG	DMSO/NA	Trypsin	TIA	9.5	3a 4
McoTI	prm	GAG	10 mM/12 h	Trypsin	TIA	6.4	3f 5
Kalata B1	wt	GL	5 mM/ 12 h	AEP	Co-elution	8.0	S9 6
AA139	wt	GL	10 mM/12 h	NH2OH	Micr	4.9	S10 7
HT-1	wt	GAG	10 mM/48 h	NA	DHFR	7.6	S11 8
Pn3a	wt	NGLP	10 mM/12 h	Carb.Y	Co-elution	5.0	S12 9
Dc1a	wt	GTGSGG	10 mM/48 h	Th.	Fly	8.9	S12 9

Disulfide connectivity and backbone cyclization (if applicable) are shown above and below the sequences, respectively; ^awt or prm denote wild type and circularly permuted N-/C-termini arrangement in the linear RGS-tagged peptide precursor; ^boxidative folding conditions are indicated as glutathione (GSH) concentration/incubation time; ^cRGS-tag removal with asparagine endopeptidase (AEP), – hydroxylamine (NH2OH), carboxypeptidase Y (Carb. Y), thrombin (Th.); ^dassay used for functionality test: trypsin-inhibitory assay (TIA), antimicrobial assay (Micr), assay based on interference with activation of dihydrofolate reductase (DHFR) (Supplementary Note 8), co-elution with folded peptide controls, insecticidal assay (Fly); ^eμM yield of POI-RGS in resin-assisted translation reaction estimated by affinity-clamp assay; ^freference to respective Supplementary Note.

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