Covalent Modification of Human Serum Albumin by the Natural Sesquiterpene Lactone ParthenolideReportar como inadecuado




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1

Institute of Pharmaceutical Technology and Biopharmacy, University of Münster, PharmaCampus, Corrensstr. 48, D-48149 Münster, Germany

2

Institute of Pharmaceutical Biology and Phytochemistry, University of Münster, PharmaCampus, Corrensstr. 48, D-48149 Münster, Germany





*

Author to whom correspondence should be addressed.



Academic Editor: Isabel C. F. R. Ferreira

Abstract The reactivity of parthenolide PRT, a natural sesquiterpene lactone from Tanacetum parthenium Asteraceae, with human serum albumin HSA was studied by UHPLC-+ESI-QqTOF MS analysis after tryptic digestion of albumin samples after incubation with this compound. It was found that the single free cysteine residue, C34, of HSA 0.6 mM reacted readily with PRT when incubated at approximately 13-fold excess of PRT 8 mM. Time-course studies with PRT and its 11β,13-dihydro derivative at equimolar ratios of the reactants revealed that PRT under the chosen conditions reacts preferably with C34 and does so exclusively via its α-methylene-γ-lactone moiety, while the epoxide structure is not involved in the reaction. View Full-Text

Keywords: sesquiterpene lactone; parthenolide; human serum albumin; tryptic digest; UHPLC-+ESI-QqTOF MS sesquiterpene lactone; parthenolide; human serum albumin; tryptic digest; UHPLC-+ESI-QqTOF MS





Autor: Michael Plöger 1, Jandirk Sendker 2, Klaus Langer 1 and Thomas J. Schmidt 2,*

Fuente: http://mdpi.com/



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