Object's details: Thermodynamic Study of Cu2+-Binding to the DAHK and GHK Peptides by Isothermal Titration Calorimetry (ITC) with the Weaker Competitor Glycine

Provider:Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Description

Title:
Thermodynamic Study of Cu2+-Binding to the DAHK and GHK Peptides by Isothermal Titration Calorimetry (ITC) with the Weaker Competitor Glycine
Creator:
Trapaidze, Ana;
Hureau, Christelle;
Bal, Wojciech;
Winterhalter, Mathias;
Faller, Peter
Description:
The peptides Asp-Ala-His-Lys (DAHK) and Gly-His-Lys (GHK) are naturally occurring copper(II)-chelating motives in human serum and cerebrospinal fluid. Here the sensitive thermodynamic technique isothermal titration calorimetry (ITC) has been used to study the energetics of copper(II) binding to DAHK and GHK peptides in the presence of the weaker ligand glycine as a competitor. DAHK and GHK bind Cu(II) predominantly in a 1:1 stoichiometry with conditional dissociation constants (i.e. at pH 7.4, in the absence of the competing chelators glycine and HEPES buffer) of 2.6 +/- 0.4 x 10-14 M and of 7.0 +/- 1.0 x 10-14 M, respectively. Furthermore, the apparent ΔH values were measured and the number of protons released upon Cu(II) binding was determined by performing experiments in different buffers. This allowed us to determine the conditional ΔG, ΔH, and ΔS, i.e. corrected for the contributions of the weaker ligand glycine and the buffer at pH 7.4. We found that the entropic and enthalpic contributions to the Cu(II)-binding to GHK and DAHK are distinct, with a higher enthalpic contribution for GHK. The obtained thermodynamic parameters correspond well to those in the literature obtained by other techniques, suggesting that the use of the weaker ligand glycine as a competitor in ITC provides accurate data for Cu(II)-binding to high affinity peptides, which cannot be accurately determined without the use of a competitor ligand.
Object availability:
free access
Date:
2012
Type:
Article;
PeerReviewed
Language:
English
Format:
application/pdf
Relation: http://eprints.ibb.waw.pl/478
Subject:
QD Chemistry
Identifier: http://eprints.ibb.waw.pl/478/1/TrapaidzeRev1final.pdf ;
Trapaidze, Ana and Hureau, Christelle and Bal, Wojciech and Winterhalter, Mathias and Faller, Peter (2012) Thermodynamic Study of Cu2+-Binding to the DAHK and GHK Peptides by Isothermal Titration Calorimetry (ITC) with the Weaker Competitor Glycine. Journal of Biological Inorganic Chemistry, 17 . 37-47.
Data provider:
Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Similar objects

Thermodynamic Study of Cu2+-Binding to the DAHK and GHK Peptides by Isothermal Titration Calorimetry (ITC) with the Weaker Competitor Glycine

Creator:Trapaidze, Ana | Hureau, Christelle | Bal, Wojciech | Winterhalter, Mathias | Faller, Peter

Date:2012

Type:other

The Final Frontier of pH and the Undiscovered Country Beyond

Creator:Bal, Wojciech | Kurowska, Ewa | Maret, Wolfgang

Date:2012.09.25

Type:other

Ternary Complex Formation and Competition Quench Fluorescence of ZnAF Family Zinc Sensors

Creator:Staszewska, Anna | Kurowska, Ewa | Bal, Wojciech

Date:2013

Type:other

Coordination properties of dithiobutylamine (DTBA), a newly introduced protein disulfide reducing agent

Creator:Adamczyk, Justyna | Bal, Wojciech | Krezel, Artur

Date:2015

Type:other

Affinity of copper and zinc ions to proteins and peptides related to neurodegenerative conditions (Aβ, APP, α-synuclein, PrP).

Creator:Zawisza, Izabela | Rózga, Małgorzata | Bal, Wojciech

Date:2012

Type:other

Electrospray-Induced Mass Spectrometry Is Not Suitable for Determination of Peptidic Cu(II) Complexes

Creator:Płonka, Dawid | Kotuniak, Radosław | Dąbrowska, Katarzyna | Bal, Wojciech

Date:2021.11.05

Type:other

Sequence-specific Ni(II)-dependent peptide bond hydrolysis for protein engineering. Combinatorial library determination of optimal sequences.

Date:2010

Type:other

The N-terminus of hepcidin is a strong and potentially biologically relevant Cu(II) chelator.

Creator:Płonka, Dawid | Bal, Wojciech

Date:2017.06.23

Type:other

Federacja Bibliotek Cyfrowych

Object's details: Thermodynamic Study of Cu2+-Binding to the DAHK and GHK Peptides by Isothermal Titration Calorimetry (ITC) with the Weaker Competitor Glycine

Description

Similar objects