Novel chemoenzymatic synthesis of peptide C-terminal amides from ester precursors
โ Scribed by Jeremy Green; Alexey L. Margolin
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- French
- Weight
- 76 KB
- Volume
- 33
- Category
- Article
- ISSN
- 0040-4039
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๐ SIMILAR VOLUMES
A new strategy for solid-phase synthesis of C-terminal peptide amides based on the use of N-tetrachlorophthaloyl protected amino acids with acid-labile side-chain protection is described.
## Abstract The standard __p__โMBHA resin used during Bocโchemistry synthesis of peptides carrying __C__โterminal carboxamides is compromised by batchโtoโbatch variations in its performance. This can cause artificially โdifficultโ couplings during peptide chain assembly, which may ultimately lead t
linkage agents useful for the so1id phase peptic synthesis of C-terminal d&s were evaluated for their relative lability toward trifluoroacetic acid. The twomst reactive linkage agents StUdied\*re cved in the synthesis of two different peptide amides by the Na-9-fluoreny~~Yloxycarbony1 protecting gro
Aminopeptidase inhibitors, phebestin, probestin and bestatin have been prepared by stereospecific reduction of ot-keto amide precursors using zinc borohydride.
The C-terminal amide group is present in several biologically active peptides including deamino-oxytocin, 1 LH\_m;\*'3 and secretin. 4 These peptides have been synthesized by solid phase methods' in which the C-terminal amide of the protected peptide was removed from the resin by amminolysis or tran