Protein‐Based Capacitive Biosensors: a New Tool for Structure‐Activity Relationship Studies |
| |
| Authors: | Alessia Mortari Natalhie Campos‐Reales Giulia Corda Nigel L Brown Elisabeth Csöregi |
| |
| Institution: | 1. Department of Analytical Chemistry, Chemical Center, P.?O. Box 124, Lund University, 221?00 Lund, Sweden;2. School of Biosciences, The University of Birmingham, Birmingham B15?2TT, U.K.;3. On leave from the Institute of Chemical Sciences, University of Bologna, Via San Donato 15, 40138, Bologna, Italy |
| |
| Abstract: | 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. |
| |
| Keywords: | MerP Menkes ATPases Wilson ATPases Affinity Receptor |
|
|
