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

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)
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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. Solid phase peptide synthesis; parallel synthesis; fluorescence-quenched substrates; protease; factor Xa.
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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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.

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