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SOLID-PHASE PEPTIDE SYNTHESIS USING MILD BASE CLEAVAGE OF NαFLUORENYLMETHYLOXYCARBONYLAMINO ACIDS, EXEMPLIFIED BY A SYNTHESIS OF DIHYDROSOMATOSTATIN
| Content Provider | Scilit |
|---|---|
| Author | Chang, Chi-Deu Meienhofer, Johannes |
| Copyright Year | 2009 |
| Description | Journal: International journal of peptide and protein research N alpha-9-Fluorenylmethyloxycarbonyl (Fmoc) amino acids will be of advantage in solid phase peptide synthesis. The Fmoc-group is quantitatively cleaved by mild base (piperidine). This permits the use of tert-butyl-type side chain blocking and of peptide-to-resin linkage cleavable by mild acidolysis. Side reactions arising from repetitive acid deprotection and final HF cleavage in contemporary solid phase synthesis are avoided. Fully bioactive and homogeneous dihydrosomatostatin was obtained in 53% overall yield. |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1399-3011.1978.tb02845.x/pdf |
| Ending Page | 249 |
| Page Count | 4 |
| Starting Page | 246 |
| ISSN | 03678377 |
| DOI | 10.1111/j.1399-3011.1978.tb02845.x |
| Journal | International journal of peptide and protein research |
| Issue Number | 3 |
| Volume Number | 11 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 2009-01-12 |
| Access Restriction | Open |
| Subject Keyword | Journal: International journal of peptide and protein research Organic Chemistry Nα‐9‐fluorenylmethyloxycarbonylamino Acids Mild Base Cleavage Mild Removal of Peptide From Solid Support Solid Phase Synthesis Tert‐butyl‐type Side Chain Protection |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry |