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Immunoreactivity and Characterization of Histidine-Rich Peptide Encapsulated Nanoclusters

Published online by Cambridge University Press:  17 March 2011

Joseph M. Slocik
Affiliation:
Department of Chemistry, VU Station B 351822, Vanderbilt University, Nashville, TN 37235-1822
Joshua T. Moore
Affiliation:
Department of Chemistry, VU Station B 351822, Vanderbilt University, Nashville, TN 37235-1822
David W. Wright*
Affiliation:
Department of Chemistry, VU Station B 351822, Vanderbilt University, Nashville, TN 37235-1822
*
Corresponding Author. Tel.: 1-615-322-2636. Fax: 1-615-343-1234 E-mail: [email protected]
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Abstract

Histidine-rich proteins (HRP), which function in the biological control of inorganic materials, have been identified in the liver fluke Fasciola hepatica, marine polychaetes, humans, and the malarial parasite Plasmodium falciparum. For example, the malarial parasite contains HRP II composed of repeating peptide sequences of Ala-His-His-Ala-His-His-AlaAla-Asp. This peptide was screened as a stabilizing peptide coat for a variety of nanoclusters of Ag0, Au0, ZnS, TiO2, and Ag2S, and characterized by UV-Vis spectroscopy, fluorescence, IR, XRD, and TEM. The resulting nanoclusters were examined for immunoreactivity against a commercial monoclonal antibody for HRP II of P. falciparum.

Type
Research Article
Copyright
Copyright © Materials Research Society 2002

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