ISSN:
1573-4943
Keywords:
Aprotinin
;
bovine pancreatic trypsin inhibitor
;
semisynthesis
;
inhibitory specificity
;
kallikrein inhibition
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract An extended concept for the replacement of amino acids in theP' region of aprotinin by chemical semisynthesis is presented. Either fragment condensation with dipeptides protected as tert-butyl ester or stepwise introduction of two single amino acid-tert-butyl esters into a partially esterified aprotinin derivative (with free Lys15-carboxyl group) lacking the amino acids Ala16 and Arg17 leads to aprotinin homologues and derivatives mutated in theP′ 1 andP′ 2 position. This method may complement the recently reported enzymatic synthesis by enabling access to aprotinin homologues and derivatives, which cannot be prepared enzymatically. The synthesis of [Ala17]BPTI and [seco-17/18]BPTI is described in detail.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01025481
Permalink
