Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds-Reference-Cited by-同舟云学术

Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds

Published:2016 Issue:4 Volume:7 Page:2666-2673
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Fehér Krisztina¹²³⁴⁵,Timári István¹²³⁴,Rákosi Kinga⁶⁷⁸⁴,Szolomájer János⁶⁷⁸⁴,Illyés Tünde Z.⁹²³⁴,Bartok Adam¹⁰²³⁴,Varga Zoltan¹⁰²³⁴¹¹,Panyi Gyorgy¹⁰²³⁴¹²,Tóth Gábor K.⁶⁷⁸⁴,Kövér Katalin E.¹²³⁴

Affiliation:

1. Department of Inorganic and Analytical Chemistry

2. University of Debrecen

3. Debrecen

4. Hungary

5. Department of Organic and Macromolecular Chemistry

6. Department of Medical Chemistry

7. University of Szeged

8. Szeged

9. Department of Organic Chemistry

10. Department of Biophysics and Cell Biology

11. MTA-DE-NAP B Ion Channel Structure-Function Research Group

12. MTA-DE Cell Biology and Signaling Research Group

Abstract

A biologically active peptide toxin containing four diselenide bonds was synthesized. The diselenide network and its dynamics were disclosed using a combined NMR and MD approach.

Funder

Országos Tudományos Kutatási Alapprogramok

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/SC/C5SC03995A

Reference46 articles.

1. K. E. Kövér and G.Batta, in Amino Acids, Peptides and Proteins: Volume 38, The Royal Society of Chemistry, 2014, vol. 38, pp. 37–59

2. Mass spectrometry-based strategies for protein disulfide bond identification

3. Comprehensive identification of disulfide bonds using non-specific proteinase K digestion and CID-cleavable crosslinking analysis methodology for Orbitrap LC/ESI-MS/MS data

4. NMR methods for determining disulfide-bond connectivities

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