Comparison of peptide precipitation in CPME, 2-MeTHF, DEE and TBME by Albericio and co-workers52.
| Peptidea | Resin | Loading (mmol g−1) | Crude yield (%) | |||
|---|---|---|---|---|---|---|
| 2-MeTHF | CPME | DEE | TBME | |||
| Leu-enkephalin (5-mer) | CTC-PS | 1.0 | 0 | 0 | 79 | 15 |
| ACP-OH (10-mer) | Wang-PS | 0.6 | 65 | 54 | 59 | 59 |
| ACP-NH2 (10-mer) | AM-Rink Amide-PS | 0.6 | 57 | 90 | 75 | 60 |
| ABRF 1992 (16-mer) | AM-Rink Amide-PS | 0.6 | 94 | 93 | 93 | 94 |
| ABRF 1992 (16-mer) | MBHA-Wang-PS | 1.1 | 100 | 95 | 100 | 100 |
| ABRF 1992 (16-mer) | MBHA-Rink Amide-PS | 1.1 | 100 | 97 | 100 | 100 |
| ABRF 1992 (16-mer) | Rink Amide-CM | 0.45 | 30 | 32 | 32 | 32 |
| ABC (20-mer) | Rink Amide-CM | 0.45 | 34 | 27 | 27 | 33 |
| Thymosin (28-mer) | AM-Rink Amide-PS | 0.6 | 74 | 75 | 75 | 72 |
a
The peptide was cleaved and deprotected using TFA/TIPS/H2O (95 : 2.5 : 2.5) (1 mL/100 mg) with shaking (1 h). The same volume of each chilled ether was added (5 × cleavage solution volume), and the solution was kept in an ice bath for 30 min. The solution was centrifuged for 5 min at 5000 rpm, and the supernatant was decanted. The procedure was repeated with a second batch of the same solvent. Residual ether was removed under a stream of N2, the solid was dissolved in water and lyophilized to determine the crude yield.