The detection of hazard exposure is a current priority, including the detection of traces of explosive molecules in different environments like luggage storage rooms and public places, and is becoming a major requirement for homeland security. In the present study we carried out a preliminary investigation on the binding capacities of four forms of the lipocalin odorant-binding protein (OBP) for the detection of explosive components such as diphenylamine, dimethyl-phthalate, resorcinol and dinitrotoluene. The experimental results, showing that OBP binds these compounds with affinity constants ranging between 80 nM and 10.6 mM, indicate that this protein can be used as a probe for the realization of a biosensor to sense explosive compounds.

The protein scaffold of the lipocalin odorant-binding protein is suitable for the design of new biosensors for the detection of explosive components.

Staiano M;Varriale A;Rossi M;D'Auria S
2007

Abstract

The detection of hazard exposure is a current priority, including the detection of traces of explosive molecules in different environments like luggage storage rooms and public places, and is becoming a major requirement for homeland security. In the present study we carried out a preliminary investigation on the binding capacities of four forms of the lipocalin odorant-binding protein (OBP) for the detection of explosive components such as diphenylamine, dimethyl-phthalate, resorcinol and dinitrotoluene. The experimental results, showing that OBP binds these compounds with affinity constants ranging between 80 nM and 10.6 mM, indicate that this protein can be used as a probe for the realization of a biosensor to sense explosive compounds.
2007
Istituto di Biochimica delle Proteine - IBP - Sede Napoli
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/125717
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