Glucosyl Platinum(II) Complexes Inhibit Aggregation of the C-Terminal Region of the Aβ Peptide.

ABSTRACT: Neurodegenerative diseases are often caused by uncontrolled amyloid aggregation. Hence, many drug discovery processes are oriented to evaluate new compounds that are able to modulate self-recognition mechanisms. Herein, two related glycoconjugate pentacoordinate Pt(II) complexes were analyzed in their capacity to affect the self-aggregation processes of two amyloidogenic fragments, Aβ_21-40 and Aβ_25-35, of the C-terminal region of the β-amyloid (Aβ) peptide, the major component of Alzheimer's disease (AD) neuronal plaques. The most water-soluble complex, 1Pt_dep, is able to bind both fragments and to deeply influence the morphology of peptide aggregates. Thioflavin T (ThT) binding assays, electrospray ionization mass spectrometry (ESI-MS), and u

SUBMITTER: La Manna S 

PROVIDER: S-EPMC9951207 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature