Table of Contents
International Journal of Proteomics
Volume 2014 (2014), Article ID 153712, 8 pages
Research Article

Dimerization of Peptides by Calcium Ions: Investigation of a Calcium-Binding Motif

1Department of Neurology, Laboratory of Neuro-Oncology, Erasmus Medical Center, 3015 GE Rotterdam, The Netherlands
2Thermo Fisher Scientific, 1046 AA Amsterdam, The Netherlands

Received 27 February 2014; Accepted 11 June 2014; Published 14 September 2014

Academic Editor: Christian Huck

Copyright © 2014 Azadeh Jamalian et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


We investigated calcium-binding motifs of peptides and their recognition of active functionalities for coordination. This investigation generates the fundamentals to design carrier material for calcium-bound peptide-peptide interactions. Interactions of different peptides with active calcium domains were investigated. Evaluation of selectivity was performed by electrospray ionization mass spectrometry by infusing solutions containing two different peptides (P1 and P2) in the presence of calcium ions. In addition to signals for monomer species, intense dimer signals are observed for the heterodimer ions ( represents the noncovalent binding of calcium with the peptide) in the positive ion mode and for ions in the negative ion mode. Monitoring of the dissociation from these mass selected dimer ions via the kinetic method provides information on the calcium affinity order of different peptide sequences.