Enforcing aggregation in a dipeptide conjugate

A bis-dipeptide scaffold (PH)2 DAB, derived from the N-terminal octa-repeats of the cellular prion protein, displayed remarkable nanoscopic self-assembly in solution. The ultrastructural details of the peptide filaments so obtained were probed by transmission electron microscopy and optical microscopy. Synthesis of the bis-dipeptide conjugate, its metalation and micrographs confirming the formation of fibrillar networks are presented.