Understanding the behavior of β-sheet proteins and their aggregation is an interesting area of study due to the possible correlation of the aggregates with neurodegenerative diseases such as Alzheimer’s disease. Studying anti-parallel β-sheet peptidomimetics could reveal information which aids in understanding the aggregation process of β-sheet proteins. The aim of this study was to determine if peptide derivatives of 2-amino-2’-carboxydiphenylacetylene maintain their β-sheet arrangement when coordinated to tungsten. In the initial investigations, peptide derivatives of 2-amino-2’-carboxydiphenylacetylene were synthesized and coordinated with tungsten to form mono-alkyne complexes. The purified complexes were examined for purity using HPLC, and their molecular composition and conformation were determined using MS and NMR. It was discovered that these complexes adopted anti-parallel β-sheet arrangements. In further work the same peptide derivatives were coordinated with tungsten to form a bis-alkyne complex <b>(A) </b>and it was examined using HPLC, MS and NMR. It was discovered that the bis-alkyne complex<b> </b>did not maintain its antiparallel β-sheet conformation. Details regarding this work will be presented.

Synthesis and evaluation of alkynyl β-sheet mimetics coordinated to tungsten

253rd National Meeting (2017)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.