Object's details: On the ability of CuAβ1-x peptides to form ternary complexes: Neurotransmitter glutamate is a competitor while not a ternary partner

Provider:Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Description

Title:
On the ability of CuAβ1-x peptides to form ternary complexes: Neurotransmitter glutamate is a competitor while not a ternary partner
Creator:
Frączyk, Tomasz;
Zawisza, Izabela;
Goch, Wojciech;
Stefaniak, Ewelina;
Drew, Simon;
Bal, Wojciech
Description:
In the light of conflicting reports on the ability of copper(II) complexes of amyloid beta (Aβ) peptides to form ternary complexes with small molecules co-present in the biological milieu, we performed a study of coordination equilibria in the system containing Cu(II) ions, the Aβ1-16 peptide, glutamic acid and 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid, HEPES) buffer. Using potentiometry, isothermal titration calorimetry (ITC), UV-visible spectroscopy and EPR, we concluded that glutamic acid was not able to form such a ternary complex, but can efficiently compete for the Cu(II) ion with the Aβ peptide at Glu concentrations relevant for the synaptic cleft. We also found that the literature constants for Cu(II) complexes with Glu were overestimated, but this effect was partially compensated by the formation of a ternary Cu(Glu)(HEPES) complex. Our results indicate that small molecules co-present with Cu(II) ions and Aβ peptides in the synaptic cleft are not very likely to enhance Cu(II)/Aβ interactions, but instead should be considered as a Cu(II) buffering system that may help prevent these interactions and participate in Cu(II) clearance from the synaptic cleft.
Object availability:
free access
Date:
2016.03
Type:
Article;
PeerReviewed
Language:
English;
eng
Format:
application/pdf
Publisher:
Elsevier
Relation: http://eprints.ibb.waw.pl/1187 ;http://www.sciencedirect.com/science/article/pii/S0162013416300617 ;
10.1016/j.jinorgbio.2016.02.035
Subject:
QD Chemistry;
QH301 Biology;
RB Pathology
Identifier: http://eprints.ibb.waw.pl/1187/1/1-s2.0-S0162013416300617-main.pdf ;
Frączyk, Tomasz and Zawisza, Izabela and Goch, Wojciech and Stefaniak, Ewelina and Drew, Simon and Bal, Wojciech (2016) On the ability of CuAβ1-x peptides to form ternary complexes: Neurotransmitter glutamate is a competitor while not a ternary partner. Journal of inorganic biochemistry . ISSN 0162-0134 (In Press)
Data provider:
Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Similar objects

On the ability of CuAβ1-x peptides to form ternary complexes: Neurotransmitter glutamate is a competitor while not a ternary partner

Date:2016.03

Type:other

A Functional Role for Aβ in Metal Homeostasis? N-Truncation and High-Affinity Copper Binding

Date:2015.07.14

Type:other

Metal assisted peptide bond hydrolysis: Chemistry, biotechnology and toxicological implications

Creator:Wezynfeld, Nina Ewa | Frączyk, Tomasz | Bal, Wojciech

Date:2016.03

Type:other

Ni(II) ions cleave and inactivate human alpha-1 antitrypsin hydrolytically, implicating nickel exposure as a contributing factor in pathologies related to antitrypsin deficiency

Creator:Wezynfeld, Nina Ewa | Bonna, Arkadiusz | Bal, Wojciech | Frączyk, Tomasz

Date:2015

Type:other

Interplay between Copper, Neprilysin, and N-Truncation of β-Amyloid

Creator:Mital, Mariusz | Bal, Wojciech | Frączyk, Tomasz | Drew, Simon

Date:2018.06.04

Type:other

Unusual Zn(II) Affinities of Zinc Fingers of Poly(ADP-ribose) Polymerase 1 (PARP-1) Nuclear Protein

Date:2015.12.30

Type:other

Human Annexins A1, A2, and A8 as Potential Molecular Targets for Ni(II) Ions

Date:2014.11.17

Type:other

Human Annexins A1, A2, and A8 as Potential Molecular Targets for Ni(II) Ions

Date:2014

Type:other

Federacja Bibliotek Cyfrowych

Object's details: On the ability of CuAβ1-x peptides to form ternary complexes: Neurotransmitter glutamate is a competitor while not a ternary partner

Description

Similar objects