Fig. 5
From: Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
Theoretical and experimental proof that increased peptide concentration reduces crystal formation. Analytical rate calculations for a TFQINS at pH 2 and b ILQINS at pH 7 showing the ratio of forward and backward rates of assembly against increasing length in the (initially dominant) c direction. c, d Compare the composition of polymorphs observed experimentally (by AFM) for the three peptides, c shows the effect of varying concentration at pH 7, and d shows the effect of varying pH at 1.5 mM. e AFM phase images of TFQINS deposited on mica self-assembled at pH 7 (5 mM) for 24 h showing splitting of crystal into two twisted fibrils. AFM 3D image f and AFM phase images g of TFQINS deposited on mica self-assembled at pH 7 (5 mM) for 24 h showing fibril-crystal transformation. AFM phase image of TFQINS deposited on h mica and i HOPG self-assembled at pH 7 (5 mM) for 24 h showing lateral aggregation (scale bar = 200 nm)
