ArticleMalaria journal2014
Chelation of Ca²⁺ ions by a peptide from the repeat region of the Plasmodium falciparum circumsporozoite protein.
Article in Malaria journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 4 citations in OpenAlex.
- Reversible Conformational Change in the Plasmodium falciparum Circumsporozoite Protein Masks Its Adhesion Domains.Infection and immunity · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundElegant efforts towards the determination of the structural tendencies of peptides derived from the Plasmodium falciparum circumsporozoite protein allowed the proposal of a left-handed helical conformation for this protein. The use of circular dichroism and Fourier-transformed infrared spectroscopy applied to various peptides derived from this protein, indicated that they bind Ca²⁺ ions in helical environments. The essential role of calcium in cell function and biological mechanisms is well known. It influences the development of several stages of the P. falciparum parasite. However, there is very little knowledge regarding calcium coordination to circumsporozoite proteins. In the present investigation the chelation of Ca²⁺ by the (NANPNVDP)₃NANP peptide, which contains the first seven 4-amino-acid blocks of the repeat region of the P. falciparum circumsporozoite protein, is tested with the use of circular dichroism and nuclear magnetic resonance spectroscopies. Spectroscopy-based solution conformations of the Ca-bound peptide are also determined.
methodsNMR spectroscopy and circular dichroism were used to test Ca²⁺ coordination by the peptide (NANPNVDP)3NANP. Solution conformations for the Ca-bound peptide were determined through molecular dynamics calculations.
resultsThe NMR spectra collected for (NANPNVDP)₃NANP indicate that the signals generated by some of the amino acids located at its C-terminal end are shifted from their original positions upon Ca²⁺ addition. The solution conformations determined for the Ca-bound peptide indicate that the metal ion can be either six- or seven-coordinate.
conclusionsThe investigation described herein strongly supports the coordination of Ca²⁺ ions to some of the amino acids located at the C-terminus of the peptide (NANPNVDP)₃NANP. The solution conformations determined for the Ca-bound congener of this peptide display many structural features associated to Ca-binding proteins.
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