Distinct Heterocyclic Moieties Govern the Selectivity of Thiophene‐Vinylene‐Based Ligands Towards Aβ or Tau Pathology in Alzheimer´s Disease

Distinct aggregated proteins are correlated with numerous neurodegenerative diseases and the development of ligands that selectively detect these pathological hallmarks is vital. Recently, synthesis thiophene‐based optical ligands, denoted bi‐thiophenevinyl‐benzothiazoles (bTVBTs), could be utilized for selective assignment tau pathology in brain tissue Alzheimer´s disease (AD) pathology, was reported. Herein, we investigate ability to distinguish deposits from amyloid‐β (Aβ), second AD associated hallmark, when replacing terminal thiophene moiety other heterocyclic motifs. The selectivity reduced introducing specific motifs, verifying molecular interactions between aggregates necessary detection deposits. In addition, having certain moieties attached central thiophene‐vinylene‐building block displayed Aβ pathology. Our findings provide chemical insights can proteinaceous species consisting different might also aid creating novel agents clinical imaging AD.