No abstract

The N‐terminal decapeptide methyl ester, H‐Ala‐Asn‐Lys‐Gly‐Phe‐Leu‐Gla‐Gla‐Val‐Arg‐OCH3(16)of bovine prothrombin fragment 1 has been prepared by standard solution techniques, via a fragment coupling strategy. Hexapeptide Boc‐Ala‐Asn‐Lyse(Boc)‐Gly‐Phe‐Leu‐OBzl (9) was obtained by coupling Boc‐Ala‐Asn‐Lyse (Boc)Gly‐OH (6)to the trifluoroacetate salt of H‐Phe‐Leu‐OBzl (8). Hydrogenolysis of(9)followed by coupling to HCl‐H‐Glaγ (OtBu)2‐Glaγ (OtBu)2‐Val‐Arg(HCl)‐OCH3(14)gave the fully protected decapeptide (15). Treatment of15with 90% trifluoroacetic acid followed by ion exchange chromatography yielded the methyl ester (16). The decapeptide16labeled with125I using the Bolton‐Hunter reagent, did not bind to antibodies specific for the calcium ion‐induced conformation of bovine fragment 1.

Das Metallbindungsverhalten von γ‐Carboxyglutaminsäure (Gla) in Peptidmodellen wird untersucht.