English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Amide proton transfer of carnosine in aqueous solution studied in vitro by WEX and CEST experiments.

MPS-Authors
/persons/resource/persons136471

Roeloffs,  V. B.
Biomedical NMR Research GmbH, MPI for Biophysical Chemistry, Max Planck Society;

External Resource
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)

2183230_Suppl.zip
(Supplementary material), 189KB

Citation

Bodet, O., Goerke, S., Behl, N. G. R., Roeloffs, V. B., Zaiss, M., & Bachert, P. (2015). Amide proton transfer of carnosine in aqueous solution studied in vitro by WEX and CEST experiments. NMR in Biomedicine, 28(9), 1097-1103. doi:10.1002/nbm.3343.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-45C0-5
Abstract
Amide protons of peptide bonds induce an important chemical exchange saturation transfer (CEST) contrast in vivo. As a simple in vitro model for a peptide amide proton CEST effect, we suggest herein the dipeptide carnosine. We show that the metabolite carnosine creates a CEST effect and we study the properties of the exchange of the amide proton (-NH) of the carnosine peptide bond (NHCPB) in model solutions for a pH range from 6 to 8.3 and a temperature range from T = 5 degrees C to 43 degrees C by means of CEST and water exchange spectroscopy (WEX) experiments on a 3 T whole-body MR tomograph. The dependence of the NHCPB chemical exchange rate k(sw) on pH and temperature T was determined using WEX. For physiological conditions (T = 37 degrees C, pH = 7.10) we obtained k(sw) = (47.07 +/- 7.90)/s. With similar chemical shift and exchange properties to amide protons in vivo, carnosine forms a simple model system for optimization of CEST pulse sequences in vitro. The potential for direct detection of the metabolite carnosine in vivo is discussed.