Side Reaction During the Deprotection of Cys(Acm)-Containing Peptides with Iodine. Synthesis of Disulfide Fragments from Cathepsin D Structure

O shift of Acm group in the serine-rich peptide III. Daughter-ion spectra of protonated molecules, recorded after collision-induced dissociation, have shown that the Acm moiety is bonded to Ser 9 or Ser 10. -->
ISSN: 1212-6950
0010-0765
DOI: 10.1135/cccc19951042
Přístupová URL adresa: https://explore.openaire.eu/search/publication?articleId=doi_________::a269870d11e4f93afe74fe511b459fa0
https://doi.org/10.1135/cccc19951042
Přírůstkové číslo: edsair.doi...........a269870d11e4f93afe74fe511b459fa0
Autor: Václav Kašička, Klaudie Bartová, Michael Mareš, Zdeněk Prusík, Jan Ježek, Karel Ubik, Vlasta Velková
Rok vydání: 1995
Předmět:
Zdroj: Collection of Czechoslovak Chemical Communications. 60:1042-1049
ISSN: 1212-6950
0010-0765
DOI: 10.1135/cccc19951042
Popis: Peptides H-TPPQC(Acm)FTV-NH2 (I) and H-VSVPC(Acm)QSASSAS-NH2 (III) were prepared by the solid phase method. Their oxidation with iodine afforded hexadecapeptide II, tetracosapeptide IV and eicosapeptide VI. The disulfide peptides II, IV and VI are designed according to the sequence of the processing loop in human cathepsin D. The purity of the peptides was determined by analytical HPLC and capillary zone electrophoresis. In addition to the expected [M + H]+ ion, FAB MS of HPLC-pure tetracosapeptide IV exhibited a molecular ion with the same relative molecular mass as the starting dodecapeptide III, in spite of clean HPLC separation of III and IV. Free-flow zone electrophoresis of IV separated peptide V, isomeric with III. Mass spectra, amino acid analysis and Edman sequencing revealed that the peptide V is a product of iodine-mediated S-->O shift of Acm group in the serine-rich peptide III. Daughter-ion spectra of protonated molecules, recorded after collision-induced dissociation, have shown that the Acm moiety is bonded to Ser 9 or Ser 10.
Databáze: OpenAIRE
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