Hydrogenation in solid phase peptide synthesis. I. removal of product from the resin
β Scribed by James M. Schlatter; Robert H. Mazur
- Publisher
- Elsevier Science
- Year
- 1977
- Tongue
- French
- Weight
- 134 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0040-4039
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
In the preceding paper,1 a description of the remwal of a peptide esterified to a polystyrene resin by means of catalytic hydrogenation was presented. This method is unique in the literature concerning solid phase peptide synthesis in that blocking groups derived frcmn A-butyl alcohol are left intac
## Synopsis Attachment of the side-chain carboxyl of the protected aspartic or glutamic acid ester to the resin support has been established for the solid-phase synthesis of the asparagine or glutamine peptide. After further elongation of the a-amino deprotected resin-bound peptide ester with prot
Ammonium for-mate aided catalytic transfer hydrogenation has been employed in the cleavage, and concommitant deprotection, of the pentapeptide leucine enkephalin from the Merrifield peptide resin under ambient conditions of temperature and pressure in a neutral medium.
Solid phase peptide synthesis a8 introduced by Merrifield' and modified by others2 is proving to be a valuable addition to the tools of the peptide chemist.