Peptide amphiphiles nanofibers with potential application in drug delivery

Self-assembly is common in organisms such as creation of double helix of DNA, lipids of cell membranes or proteins quaternary structure. It is well known that electrically charged sites can bind and concentrate amino acids and presence of metal ions can accelerate the condensation reaction, linking the monomers to form polymers and other complex structures. Recently, this method of self-assembly has been frequently used for nanofibers, which cannot be obtained by other methods for the nanofibers production, such as electrospinning (e.g. cellulose nanofibers).

One of the recently published papers deals with the nanofibers from peptides that can serve as biodegradable vehicles for drug delivery or release. Peptide amphiphiles (PA) are peptide-based molecules that self-assemble into high aspect ratio nanofibers. These structures were first described by Samuel I. Stupp group from the Northwestern University in 2003. These molecules   have three areas usually: the hydrophobic tail region, b-sheet consisting of amino acids and peptide epitope, whose aim is to allow the molecules dissolve in water, and to fulfil the biological function of interaction with living systems. The publication describes the synthesis of four self-sssembling peptide amphiphiles. Prodan (6-propionyl-2-dimethylaminonaphtalene) was used as a dye for observation of its release from nanofibers in gel form.  The kinetics of release was observed and it was found that release half-lives depended on the fluorophore position in the PA sequence.

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^{http://pubs.rsc.org/en/content/articlelanding/2012/sm/c2sm07420f}