Resolution of proline acylation problem for thiol capture strategy by use of a chloro-dibenzofuran template.
Int J Pept Protein Res
; 40(2): 141-7, 1992 Aug.
Article
en En
| MEDLINE
| ID: mdl-1280251
ABSTRACT
The acyl transfer rate for proline, in the prior thiol capture strategy, was enhanced by changing the electronic character of the dibenzofuran template. The rate of amide bond formation between proline and cysteine by the 1-chloro-4-hydroxy-6-mercaptodibenzofuran was measured to be 0.012 min-1, which translates to a half-life of 53 min. Further enhancement of the reaction rate was accomplished by the use of a 1,3-dichloro-dibenzofuran template. The k1 for the reaction was measured to be 0.093 min-1, and the half-life was calculated to be 7 min. To test the applicability of the activated template, 1-chloro-4-hydroxy-6-mercaptodibenzofuran, in peptide synthesis, the 34 amino acid long peptide, H-RPDFCLEPPYTGPCRKARNNFKSADECMRTCGGA-OH, was synthesized. This peptide represents the condensation of the N-terminal 13-mer and the C-terminal 21-mer of the basic pancreatic trypsin inhibitor.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Compuestos de Sulfhidrilo
/
Benzofuranos
/
Prolina
Idioma:
En
Revista:
Int J Pept Protein Res
Año:
1992
Tipo del documento:
Article