Table of Contents
Molecules, Volume 24, Issue 11 (June-1 2019)
- Issues are regarded as officially published after their release is announced to the table of contents alert mailing list.
- You may sign up for e-mail alerts to receive table of contents of newly released issues.
- PDF is the official format for papers published in both, html and pdf forms. To view the papers in pdf format, click on the "PDF Full-text" link, and use the free Adobe Reader to open them.
Cover Story (view full-size image) Amyloid-β peptide (Aβ) is an intrinsically disordered protein (IDP). Its aggregation into toxic [...] Read more. Amyloid-β peptide (Aβ) is an intrinsically disordered protein (IDP). Its aggregation into toxic oligomers and amyloid fibrils is one of the hallmarks of Alzheimer’s disease (AD). The all-
D-enantiomeric peptide D3 was developed based on the rationale that stabilizing Aβ in its monomeric IDP conformation efficiently inhibits the formation of toxic Aβ assemblies. Using microscale thermophoresis and analytical ultracentrifugation, the present study demonstrated that D3 directly interacts with Aβ42 monomers with nanomolar affinity, leading to the formation of highly dynamic complexes at various stoichiometries. The transient interaction of D3 at clearly substoichiometric ratios retains Aβ42 monomers in disordered conformations and delays the formation of Aβ assemblies. View this paper.