Cu(ii)-catalyzed C-N coupling of 2-aminobenzothiazoles with boronic acids at room temperature.

A Cu(ii)-catalyzed, effective C-N coupling of 2-aminobenzothiazoles with boronic acids in acetonitrile under open vessel chemistry was achieved. This protocol demonstrates the -arylation of 2-aminobenzothiazoles with a broad range of differently substituted phenylboronic acids at room temperature and accomplishes moderate to excellent yields of the desired products. Under the optimized condition, phenylboronic acids bearing halogen at the and positions were found to be more fruitful.

Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents.

Several amyloid-forming proteins are characterized by the presence of hydrophobic and highly amyloidogenic core sequences that play critical roles in the initiation and progression of amyloid fibril formation. Therefore targeting these sequences represents a viable strategy for identifying candidate molecules that could interfere with amyloid formation and toxicity of the parent proteins. However, the highly amyloidogenic and insoluble nature of these sequences has hampered efforts to develop high-throughput fibrillization assays.

Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis.

The study of conformational transitions of peptides has obtained considerable attention recently because of their importance as a molecular key event in a variety of degenerative diseases. However, the study of peptide self-assembly into beta-sheets and amyloid beta (Abeta) fibrils is strongly hampered by their difficult synthetic access and low solubility. We have recently developed a new concept termed switch-peptides that allows the controlled onset of polypeptide folding and misfolding at physiologic conditions.

Switch-peptides: controlling self-assembly of amyloid beta-derived peptides in vitro by consecutive triggering of acyl migrations.

The sequential triggering (Soff --> Son) of O, N-acyl migrations (AcM) by chemical and enzymatic methods (Ti) in peptides containing structure-disrupting switch-elements, S (switch-peptides), offers a novel tool for studying in statu nascendi the onset and inhibition of polypeptide folding and self-assembly as a key process in degenerative diseases.