Tuning the coordination properties of multi-histidine peptides by using a tripodal scaffold: solution chemical study and catechol oxidase mimicking-Reference-Cited by-同舟云学术

Tuning the coordination properties of multi-histidine peptides by using a tripodal scaffold: solution chemical study and catechol oxidase mimicking

Published:2017 Issue:2 Volume:41 Page:808-823
ISSN:1144-0546
Container-title:New Journal of Chemistry
language:en
Short-container-title:New J. Chem.

Author:

Dancs Ágnes¹²³⁴⁵,May Nóra V.⁶⁷⁴,Selmeczi Katalin⁵⁸⁹¹⁰,Darula Zsuzsanna¹¹¹²¹³¹⁴⁴^ORCID,Szorcsik Attila¹⁵³⁴,Matyuska Ferenc¹²³⁴,Páli Tibor¹⁶¹²¹³¹⁴⁴,Gajda Tamás¹²³⁴

Affiliation:

1. Department of Inorganic and Analytical Chemistry

2. University of Szeged

3. H-6720 Szeged

4. Hungary

5. Université de Lorraine – CNRS

6. Research Centre for Natural Sciences HAS

7. H-1117 Budapest

8. UMR 7565 SRSMC

9. 54506 Vandœuvre-lès-Nancy

10. France

11. Institute of Biochemistry

12. Biological Research Centre

13. Hungarian Academy of Sciences

14. H-6724 Szeged

15. MTA-SZTE Bioinorganic Chemistry Research Group

16. Institute of Biophysics

Abstract

Histidine-rich tripodal peptides form unique oligonuclear complexes with copper(ii), which exhibit efficient catecholase-like activity.

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,General Chemistry,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2017/NJ/C6NJ03126A

Reference91 articles.

1. Proton and Metal Ion Interactions with Glycylglycylhistamine, a Serum Albumin Mimicking Pseudopeptide

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3. The dimeric and tetrameric octarepeat fragments of prion protein behave differently to its monomeric unit

4. Identification of a novel high affinity copper binding site in the APP(145–155) fragment of amyloid precursor protein

5. Copper(II) Interaction with Prion Peptide Fragments Encompassing Histidine Residues Within and Outside the Octarepeat Domain: Speciation, Stability Constants and Binding Details

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