Peptide amphiphiles (PAs) are novel engineered biomaterials able to self-assemble into supramolecular
systems that have shown significant promise in drug delivery across the cell membane
and across challenging biological barriers showing promise in the field of brain diseases, regenerative
medicine and cancer. PAs are amino-acid block co-polymers, with a peptide backbone composed usually
of 8-30 amino acids, a hydrophilic block formed by polar amino acids, a hydrophobic block
which usually entails either non-polar or aromatic amino acids and alkyl, acyl or aryl lipidic tails and
in some cases a spacer or a conjugated targeting moiety. Finely tuning the balance between the hydrophilic
and hydrophobic blocks results in a range of supramolecular structures that are usually stabilised by hydrophobic,
electrostatic, β-sheet hydrogen bonds and π-π stacking interactions. In an aqueous environment, the final size, shape and
interfacial curvature of the PA is a result of the complex interplay of all these interactions. Lanreotide is the first PA to be
licensed for the treatment of acromegaly and neuroendocrine tumours as a hydrogel administered subcutaneously, while a
number of other PAs are undergoing preclinical development. This review discusses PAs architecture fundamentals that
govern their self-assembly into supramolecular systems for applications in drug delivery.
Keywords: Peptide amphiphiles, Peptide self-assembly, Driving forces, Drug delivery, Nanofibers.
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