Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  Preserving catalytic activity and enhancing biochemical stability of the therapeutic enzyme asparaginase by biocompatible multi layered polyelectrolyte microcapsules.

Karamitros, C. S., Yashchenok, A. M., Moehwald, H., Skirtach, A. G., & Konrad, M. (2013). Preserving catalytic activity and enhancing biochemical stability of the therapeutic enzyme asparaginase by biocompatible multi layered polyelectrolyte microcapsules. Biomacromolecules, 14(12), 4398-4406. doi:10.1021/bm401341k.

Item is

Dateien

einblenden: Dateien
ausblenden: Dateien
:
1878006.pdf (Verlagsversion), 3MB
Name:
1878006.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
application/pdf / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-
:
1878006_Suppl_1.pdf (Ergänzendes Material), 809KB
Name:
1878006_Suppl_1.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
application/pdf / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-

Externe Referenzen

einblenden:
ausblenden:
externe Referenz:
http://pubs.acs.org/doi/pdf/10.1021/bm401341k (Verlagsversion)
Beschreibung:
-
OA-Status:

Urheber

einblenden:
ausblenden:
 Urheber:
Karamitros, C. S.1, Autor           
Yashchenok, A. M., Autor
Moehwald, H., Autor
Skirtach, A. G., Autor
Konrad, M.1, Autor           
Affiliations:
1Research Group of Enzyme Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578612              

Inhalt

einblenden:
ausblenden:
Schlagwörter: -
 Zusammenfassung: The present study focuses on the formation of microcapsules containing catalytically active L-asparaginase (L-ASNase), a protein drug of high value in antileukemic therapy. We make use of the layer-by-layer (LbL) technique to coat protein-loaded calcium carbonate (CaCO3) particles with two or three poly dextran/poly-L-arginine-based bilayers. To achieve high loading efficiency, the CaCO3 template was generated by coprecipitation with the enzyme. After assembly of the polymer shell, the CaCO3 core material was dissolved under mild conditions by dialysis against 20 mM EDTA. Biochemical stability of the encapsulated L-asparaginase was analyzed by treating the capsules with the proteases trypsin and thrombin, which are known to degrade and inactivate the enzyme during leukemia treatment, allowing us to test for resistance against proteolysis by physiologically relevant proteases through measurement of residual L-asparaginase activities. In addition, the thermal stability, the stability at the physiological temperature, and the long-term storage stability of the encapsulated enzyme were investigated. We show that encapsulation of L-asparaginase remarkably improves both proteolytic resistance and thermal inactivation at 37 degrees C, which could considerably prolong the enzyme's in vivo half-life during application in acute lymphoblastic leukemia (ALL). Importantly, the use of low EDTA concentrations for the dissolution of CaCO3 by dialysis could be a general approach in cases where the activity of sensitive biomacromolecules is inhibited, or even irreversibly damaged, when standard protocols for fabrication of such LbL microcapsules are used. Encapsulated and free enzyme showed similar efficacies in driving leukemic cells to apoptosis.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2013-10-212013-12
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1021/bm401341k
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Biomacromolecules
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 14 (12) Artikelnummer: - Start- / Endseite: 4398 - 4406 Identifikator: -