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Protein-Based Capacitive Biosensors: a New Tool for Structure-Activity Relationship Studies

Mortari, Alessia LU ; Campos-Reales, Natalhie; Corda, Giulia; Brown, Nigel L. and Csöregi, Elisabeth LU (2008) In Electroanalysis 20(24). p.2677-2684
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
MerP, Affinity, Wilson ATPases, Menkes ATPases, Receptor
in
Electroanalysis
volume
20
issue
24
pages
2677 - 2684
publisher
John Wiley & Sons
external identifiers
  • wos:000261876800012
  • scopus:57849125976
ISSN
1040-0397
DOI
10.1002/elan.200604400
language
English
LU publication?
yes
id
4f74c690-9865-485d-98f7-2d459b9e1add (old id 1377459)
date added to LUP
2009-04-24 09:36:54
date last changed
2017-03-19 03:54:55
@article{4f74c690-9865-485d-98f7-2d459b9e1add,
  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.},
  author       = {Mortari, Alessia and Campos-Reales, Natalhie and Corda, Giulia and Brown, Nigel L. and Csöregi, Elisabeth},
  issn         = {1040-0397},
  keyword      = {MerP,Affinity,Wilson ATPases,Menkes ATPases,Receptor},
  language     = {eng},
  number       = {24},
  pages        = {2677--2684},
  publisher    = {John Wiley & Sons},
  series       = {Electroanalysis},
  title        = {Protein-Based Capacitive Biosensors: a New Tool for Structure-Activity Relationship Studies},
  url          = {http://dx.doi.org/10.1002/elan.200604400},
  volume       = {20},
  year         = {2008},
}