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Protein‐Based Capacitive Biosensors: a New Tool for Structure‐Activity Relationship Studies
Author(s) -
Mortari Alessia,
CamposReales Natalhie,
Corda Giulia,
Brown Nigel L.,
Csöregi Elisabeth
Publication year - 2008
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.200604400
Subject(s) - chemistry , biosensor , periplasmic space , cysteine , biochemistry , combinatorial chemistry , metalloprotein , enzyme , escherichia coli , gene
The present work reports a new application of a protein‐based capacitive biosensor as an in vitro assay for the selectivity study of the bacterial periplasmic protein MerP and four MerP variants. The modified MerP proteins were produced by site‐directed mutagenesis of the heavy metal associated motif (HMA). The MerP and modified MerPs selectivity for copper, zinc, cadmium and mercury bivalent ions were investigated and compared. The variations in the proteins affinity were related to the primary structure of the HMA motifs. Key amino acids for copper coordination of metalloproteins that contain the metal binding sequence Gly‐Met‐Thr‐Cys‐xxx‐xxx‐Cys were identified. The results brought insights valid for Menkes and Wilson ATPases. The protein‐based capacitive biosensors were a simple and useful tool for studying structure‐activity relationships of proteins.