Furthermore, a detailed analysis of 2D NOESY spectra of peptide p1 did not reveal any crosspeaks between H N atoms of the peptide, suggesting no preferable stable conformation of the backbone in the aggregated and low-oligomeric states. In contrast to peptide p1, even at the highest used concentration of 1.5 mM, H N groups of residues Arg1, Arg2, Arg4, Dip5, and Dip7 in peptide p3 demonstrate strong exchange cross-peaks with water in TOCSY spectra (Figure ). These cross-peaks, as well as the H N signal linewidths (around 8-10 Hz), indicate that p3 exists in a low-oligomeric state, with its backbone partially exposed to solvent. Peptide 15c demonstrates behavior similar to p3 at all tested concentrations, with linewidths below 8 Hz, which corresponds to the monomeric (or very low oligomeric) form of the peptide. Additionally, exchange cross-peaks with water were detected for the backbone H N groups of Arg2 and Arg4 at both tested concentrations (Figure ).