synthesis of novel peptides using unusual amino acids

Small peptides are valuable peptides due to their extended biological activities. their activities could be categorized according to their low antigenicity, osmotic pressure, and also because of their astonishing bioactivities. for example, the aggression of phe-phe fibers via self-assembly and intermolecular hydrogen bonding is the main reason for the formation of alzheimer’s β-amyloid fibrils. hydrogen bonding is the main intramolecular interaction in peptides, while the presence of aromatic ring leads to the π-π stacking and affects the self-assembly and aggression. thus, insertion of an unusual amino acid into peptide sequence facilitates the formation of intramolecular bonds, lipophilicity and its conformation. to design new small peptides with remarkable lipophilicity, it is an idea to employ γ-amino acid, such as gabapentin (h2n-gpn- ome) and baclofen (h2n-baclofen-ome), in the structure of small peptides to increase cellpenetrating properties and to prevent aggression of phe-phe fibrils in β-amyloids of alzheimer’s disease. some new tri- and tetrapeptides were synthesized through introducing biologically active gabapentin and baclofen to dipeptide of phenylalanine (phe-phe) through solution phase peptide synthesis strategy.