TABLE 1.
RPP cleaves basic peptides
| Peptidea | Peptide sequence and sites of cleavage by RPPb | Degradationc (%) | Net charged |
|---|---|---|---|
| A | YGGF↓LRR↓IRP↓K↓L↓KWDNQ | 76.4 | +4 |
| B | HSDAVFTDN↓YT↓R↓L↓RKQ↓M↓ AKKYLNSILN | 36.2 | +3 |
| C | INLKA↓LAA↓LAK↓KIL | 7.2 | +3 |
| D | Ac-SYSMEH↓F↓RWGKPV-NH2 | 15.7 | +1 |
| E | VNTPEHVVPYGLGSPRS | <1.0 | 0 |
| F | CETQRTLLNGDLQTSI | <1.0 | −1 |
| G | LENLEAETAPLP | <1.0 | −3 |
| H | Pyr-GPWLEEEEEAYGWMDF-NH2 | <1.0 | −6 |
a
Peptide A, dymorphin A; B, vasoactive intestinal peptide; C, mastoparan; D, αMSH amide; E, big endotheline; F, peptide fragment of somatostatin receptor SSTR2A; G, peptide fragment of μ opioid receptor MOR1A; H, gastrin I.
b
Arrows denote RPP cleavage sites for peptides, which were identifiable. Basic residues are indicated in italics.
c
Cleavage efficiencies are determined as described in Materials and Methods.
d
Net charges are caluculated from acidic and basic amino acid residues in each peptide in the reaction condition.