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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Cotton Chemistry and Utilization Research » Research » Publications at this Location » Publication #303747
Title: Elastase kinetics and structural features of colorimetric and fluorescent peptides on cellulose nanocrystals

Author
item Prevost, Nicolette
item Edwards, Judson - Vince
item French, Alfred - Al
item Concha, Monica
item Condon, Brian

Submitted to: American Chemical Society National Meeting
Publication Type: Abstract Only
Publication Acceptance Date: 10/28/2013
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Human neutrophil elastase (HNE) and porcine pancreatic elastase (PPE) are serine proteases with destructive proteolytic activity. Because of this activity, there is considerable interest in elastase sensors. Herein we report the synthesis, characterization, and kinetic profiles of tri- and tetrapeptide substrates of elastase as glycine-esterified fluorescent and colorimetric analogs of cotton cellulose nanocrystals (CCN). The degree of substitution of peptide incorporated in CCN was 3-4 peptides per 100 anhydroglucose units. Glycine and peptide-cellulose-nanocrystals revealed a crystallite size of 58.5 Å. A crystallite model of the peptide-cellulose conjugate is shown with a view to how elastase may interact on the transducer surface. The sensor limits of detection at 2 mg of the tri- and tetrapeptide CCN conjugates over a 10 minute reaction time course were 0.03 U/mL PPE and 0.05 U/mL HNE respectively.