(Q57816817)

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Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine

article published in 2011

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scholarly article

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Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine (English)

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1 reference

ChEBI release 2020-05-28

object named as

Peter Faller

5

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Mathias Winterhalter

object named as

Mathias Winterhalter

4

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3

object named as

Wojciech Bal

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author name string

Ana Trapaidze

1

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Christelle Hureau

2

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publication date

4 September 2011

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Journal of Biological Inorganic Chemistry

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17

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1

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37-47

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The Cu(II)/Abeta/human serum albumin model of control mechanism for copper-related amyloid neurotoxicity

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Asp-Ala-His-Lys (DAHK) inhibits copper-induced oxidative DNA double strand breaks and telomere shortening

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An analog of the human albumin N-terminus (Asp-Ala-His-Lys) prevents formation of copper-induced reactive oxygen species

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Copper transfer from Cu-Abeta to human serum albumin inhibits aggregation, radical production and reduces Abeta toxicity.

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The human tri-peptide GHK and tissue remodeling

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Three histidine residues of amyloid-beta peptide control the redox activity of copper and iron

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Copper complexes of glycyl-histidyl-lysine and two of its synthetic analogues: chemical behaviour and biological activity

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Thermodynamic and spectroscopic study of Cu(II) and Ni(II) binding to bovine serum albumin

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Quantification of the binding constant of copper(II) to the amyloid-beta peptide

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Determining thermodynamic parameters from isothermal calorimetric isotherms of the binding of macromolecules to metal cations originally chelated by a weak ligand

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Structural and thermodynamical properties of CuII amyloid-beta16/28 complexes associated with Alzheimer's disease.

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Cu(II) complexation by "non-coordinating" N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid (HEPES buffer).

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Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition

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Synthesis of the native copper(II)-transport site of human serum albumin and its copper(II)-binding properties

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Direct measurement of protein binding energetics by isothermal titration calorimetry

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Spectropotentiometric analysis of metal binding to structural zinc-binding sites: accounting quantitatively for pH and metal ion buffering effects.

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The interaction of copper(II) and glycyl-l-histidyl-l-lysine, a growth-modulating tripeptide from plasma

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Isothermal titration calorimetry measurements of Ni(II) and Cu(II) binding to His, GlyGlyHis, HisGlyHis, and bovine serum albumin: a critical evaluation

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Speciation and structure of copper(II) complexes with histidine-containing peptides in aqueous medium: a combined potentiometric and spectroscopic study

1 reference

https://pubmed.ncbi.nlm.nih.gov/21898044

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based on heuristic

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Structure of the glycyl-L-histidyl-L-lysine-copper(II) complex in solution

1 reference

https://pubmed.ncbi.nlm.nih.gov/21898044

12 December 2020

based on heuristic

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Short peptides are not reliable models of thermodynamic and kinetic properties of the N-terminal metal binding site in serum albumin

1 reference

https://pubmed.ncbi.nlm.nih.gov/21898044

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Ternary Coordination Complex between Human Serum Albumin, Copper (II), and l-Histidine

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Characterization of the copper(II)- and nickel(II)-transport site of human serum albumin. Studies of copper(II) and nickel(II) binding to peptide 1-24 of human serum albumin by 13C and 1H NMR spectroscopy

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Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride

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https://pubmed.ncbi.nlm.nih.gov/21898044

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Application of isothermal titration calorimetry in bioinorganic chemistry

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https://pubmed.ncbi.nlm.nih.gov/21898044

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Human serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity

1 reference

https://pubmed.ncbi.nlm.nih.gov/21898044

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1007/S00775-011-0824-5

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