Table 1.
Characterization of peptides.
| no. | peptides | ring size | % purity | tRc min | MSd (M + H)+ | ||
|---|---|---|---|---|---|---|---|
| HPLCa | CZEb | calcd. | obsd. | ||||
| 7 | cyclo(2-7)[DPhe1-Cys2-Phe3-DTrp4-Lys5-Thr6-Cys7-Thr8-NH2] (Octreotide-amide) | 20 | 99 | 99 | 17.4 | 1032.436 | 1032.404 |
| 8 | DPhe1-Ncy(tBu2-Phe3-DTrp4-Lys5-Thr6-Ncy(tBu)7-Thr8-NH2 | - | 98 | 99 | 35.8 | 1118.546 | 1118.502 |
| 9 | cyclo(2-7)[DPhe1-Ncy2-Phe3-DTrp4-Lys5-Thr6-Ncy7-Thr8-NH2] | 18 | 99 | 99 | 14.9 | 1004.405 | 1004.341 |
Percentage purity determined by HPLC using buffer A: TEAP, pH 2.30, buffer B: 60% CH3CN/40% A under gradient conditions (20% to 50% B over 30 min), at flow rate of 0.2 mL/min on a Vydac C18 column (0.21 cm × 15 cm, 5 μm particle size, 300 Å pore size). Detection at 214 nm.
Percentage purity determined by capillary zone electrophoresis (CZE) using a Beckman P/ACE System 2050 controlled by an IBM Personal system/2 model 50Z; field strength of 15 kV at 30 °C. Buffer, 100 mM sodium phosphate (85:15, H2O:CH3CN), pH 2.50, on a Agilent μSil bare fused-silica capillary (75 μm i.d. × 40 cm length). Detection at 214 nm.
Retention times under HPLC conditions described above.
Mass spectra (MALDI-MS) were measured on an ABI-Voyager DE-STR instrument using saturated solution of α-cyano-4-hydroxycinnamic acid in 0.3% trifluoroacetic acid and 50% acetonitrile as matrix. The calculated [M + H] of the monoisotope was compared with the observed [M + H]+ monoisotopic mass.