Naslov
Proteolytic stability of the peptide PL 14736

Autori
Stipaničić, Siniša ; Mildner, Boris

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Congress of the Croatian Society of Biochemistry and Molecular Biology with international participation ; HDBMB 2004, Book of Abstracts / Dumić, Jerka - Zagreb : Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu, 2004, 152-152

Skup
Congress of the Croatian Society of Biochemistry and Mlecular Biology

Mjesto i datum
HOC Bjelolasica, Hrvatska, 30.09.2004. - 02.10.2004

Vrsta sudjelovanja
Poster

Vrsta recenzije
Domaća recenzija

Ključne riječi
mass spectrometry; plasma; serum; blood; proteolytic stability; PL 14736

Sažetak
The aim of the study was to determine proteolytic stability of the peptide PL 14736 (GEPPPGKPADDAGLV) in human plasma, serum and blood. Methods: The stabilities of the intact peptide and its derivatives, where alanine was substituted with amino acids at different positions of the peptide's primary sequence, were studied in biological fluids. Hydrolysis products of the peptide in buffered solutions of elastase, trypsin, chymotrypsin, pepsin and aminopeptidase, were also monitored. In all hydrolysis experiments, peptide analysis were performed by tandem mass spectrometry (QTOF). Results: The hydrolysis of N-terminal amino acid (Gly) was detected in biological fluids. This was found to be due to the enzymatic activity of the aminopeptidase, since acetylation of the N-terminal amino acid completly stabilized the peptide in human sera and plasma. By comparing the hydrolytic stability of the PL 14736 peptide and its derivatives (where prolines were substituted with alanines) in human sera and plasma it was shown that three consecutive prolines in the PL 14736 primary structure have a major influence on its proteolytic stability.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija, Farmacija

Napomena
Rad je izrađen i financiran od PLIVA Istraživački Institut d.o.o.

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