Wydział Chemii

Aleksandra Hecel

Sara Draghi

Daniela Valensin

Henryk Kozłowski

2017

Dalton Transactions

46

7758-7769

10.1039/c7dt01069a

Naukowa

Angielski

Artykuł

Prion proteins (PrP) from different species have the ability to tightly bind Cu2+ions. Copper coordinationsites are located in the disordered andflexible N-terminal region which contains several His anchoringsites. Among them, two His residues are found in the so called amyloidogenic PrP region which isbelieved to play a key role in the process leading to oligomer andfibril formation. Both chicken andhuman amyloidogenic regions have a hydrophobic C-terminal region rich in Ala and Val amino acids.Recentfindings revealed that this domain undergoes random coil toα-helix structuring upon interactionwith membrane models. This interaction might strongly impact metal binding abilities either in terms ofdonor sets or affinity. In this study we investigated Cu2+interaction with an amyloidogenic fragment,chPrP105–140, derived from chicken prion protein (chPrP), in different solution environments. The be-havior of the peptide and its metal complexes was analyzed in water and in the presence of negative andpositive charged membrane mimicking environments formed by sodium dodecyl sulfate (SDS) anddodecyl trimethyl ammonium chloride (DTAC) micelles. The metal coordination sphere, the metal bindingaffinity and stoichiometry were evaluated by combining spectroscopic and potentiometric methods.Finally we compare copper(II) interactions with human and chicken amyloidogenic fragments. Our resultsindicate that the chicken amyloidogenic fragment is a stronger copper ligand than the human amyloido-genic fragment.

CC-BY

http://dx.doi.org/10.1039/c7dt01069a

https://www.rsc.org/