English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Sialorphin and its analog as ligands for copper(II) ions.

Kamysz, E., Kotynia, A., Czyznikowska, Z., Jaremko, M., Jaremko, L., Nowakowski, M., et al. (2013). Sialorphin and its analog as ligands for copper(II) ions. Polyhedron, 55, 216-224. doi:10.1016/j.poly.2012.10.055.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-F4B8-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C7E3-0
Genre: Journal Article

Files

show Files
hide Files
:
1795903.pdf (Publisher version), 2MB
 
File Permalink:
-
Name:
1795903.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), Göttingen; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Kamysz, E., Author
Kotynia, A., Author
Czyznikowska, Z., Author
Jaremko, M.1, Author              
Jaremko, L.1, Author              
Nowakowski, M., Author
Brasun, J., Author
Affiliations:
1Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              

Content

show
hide
Free keywords: Sialorphin Peptides Copper(II) ion Metal ions complexes Synthesis Potentiometry Stability constants UV–Vis CD NMR Theoretical calculations
 Abstract: In this study the sialorphin (Gln-His-Asn-Pro-Arg) and its analog (Glp-His-Asn-Pro-Arg) were analyzed in terms of metal binding ability. Both peptides were synthesized using the solid-phase method. The application of number analytical methods: potentiometry, spectroscopy (UV-Vis, CD, NMR) and mass spectrometry allowed for a detailed characterization of the coordination abilities of presented peptides. The analysis of the obtained results has shown that both peptides are able to form a series of complexes. However due to the presence of free N-terminal amino group the sialorphin is more effective in metal ion binding. Nevertheless, in basic conditions both peptides involve the amide nitrogen belonging to the side chain of Asn3 moiety and form 4N complex with square planar structure. This unusual ability has been confirmed by the results obtained from the NMR studies.

Details

show
hide
Language(s): eng - English
 Dates: 2013-03-202013-05-17
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.poly.2012.10.055
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Polyhedron
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 55 Sequence Number: - Start / End Page: 216 - 224 Identifier: -