A novel, bimetallic ring system adopts and maintains a rigid conformation has recently been discovered. This organometallic ring system possesses a ferrocene complex at one end and a tungsten bis-alkyne complex at the other end. Although an X-ray structure of this molecule has yet to be obtained, DFT calculations indicate that the two alkynes are roughly parallel to each other and separated by a distance of approximately 3.5 Å. Since the peptide strands in a β-sheet are separated by 3.3 Å, it has been proposed that peptides linked to the two alkynes in this rigid organometallic ring will adopt a β-sheet structure. If these molecules do adopt β-sheet conformations, then they have the potential to serve as model systems for studying the forces that maintain or disrupt β-sheets, information that would help biomedical researchers investigating diseases (like Alzheimer's disease) that appear to be mediated by formation of β-sheet proteins. This presents a unique opportunity for inorganic chemistry to potentially address a pressing issue in biochemistry and medicine. To test this hypothesis, 1 and molecules having the general structure 2 have been prepared and examined. The amino acids in 2 are linked to the rigid ring system via the two alkynes using a methyleneamine spacer. This presentation will detail the how these complexes have been prepared, how their solution conformation has been probed using NMR spectroscopy, and how information about their conformation has been obtained using DFT calculations.

Peptides linked via a methyleneamine linker to a rigid, bimetallic ring system as a possible model system for β-sheet formation

255th National Meeting (2018)

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