Molecules 2004, 9(6), 427-439; doi:10.3390/90600427
Article

The Preparation of Fluorescence-Quenched Probes for Use in the Characterization of Human Factor Xa Substrate Binding Domains

1 Centre for Green Chemistry, Monash University, Clayton, Victoria, 3800. Australia 2 2 School of Chemistry, Monash University, Clayton, Victoria, 3800. Australia 3 2 3 CSIRO Molecular Science, Private Bag 10, Clayton South, Vic 3169, Australia
* Author to whom correspondence should be addressed.
Received: 4 March 2004; Accepted: 14 March 2004 / Published: 31 May 2004
(This article belongs to the Special Issue RACI 2003 symposium)
PDF Full-text Download PDF Full-Text [212 KB, uploaded 20 June 2008 16:51 CEST]
Abstract: The preparation and characterization by LCMS of a library of 55 fluorescence- quenched peptides is described. The peptides bear a terminal anthranilamide fluorophore and a penultimate 2,4-dinitrophenyl-L-lysine quencher, and will be used to probe the substrate binding domain of the human blood coagulation enzyme, factor Xa.
Keywords: Solid phase peptide synthesis; parallel synthesis; fluorescence-quenched substrates; protease; factor Xa.

Article Statistics

Load and display the download statistics.

Citations to this Article

Cite This Article

MDPI and ACS Style

Bromfield, K.M.; Cianci, J.; Duggan, P.J. The Preparation of Fluorescence-Quenched Probes for Use in the Characterization of Human Factor Xa Substrate Binding Domains. Molecules 2004, 9, 427-439.

AMA Style

Bromfield KM, Cianci J, Duggan PJ. The Preparation of Fluorescence-Quenched Probes for Use in the Characterization of Human Factor Xa Substrate Binding Domains. Molecules. 2004; 9(6):427-439.

Chicago/Turabian Style

Bromfield, Karen M.; Cianci, Julia; Duggan, Peter J. 2004. "The Preparation of Fluorescence-Quenched Probes for Use in the Characterization of Human Factor Xa Substrate Binding Domains." Molecules 9, no. 6: 427-439.

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert