Interaction between Hemin and Prion Peptides: Binding, Oxidative Reactivity and Aggregation.

ABSTRACT: We investigate the interaction of hemin with four fragments of prion protein (PrP) containing from one to four histidines (PrP106-114, PrP95-114, PrP84-114, PrP76-114) for its potential relevance to prion diseases and possibly traumatic brain injury. The binding properties of hemin-PrP complexes have been evaluated by UV-visible spectrophotometric titration. PrP peptides form a 1:1 adduct with hemin with affinity that increases with the number of histidines and length of the peptide; the following log K1 binding constants have been calculated: 6.48 for PrP76-114, 6.1 for PrP84-114, 4.80 for PrP95-114, whereas for PrP106-114, the interaction is too weak to allow a reliable binding constant calculation. These constants are similar to that of amyloid-β (Aβ) for hemin, and similarly to hemin-A

SUBMITTER: Dell'Acqua S 

PROVIDER: S-EPMC7589926 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature