A new class of promising drug carriers based on collagen mimetic peptides assembled into triplehelical peptide (THP) is described. The peptides fold into a triple helical conformation forminghigh aspect ratio, rigid rod nanoparticles. The fluorescein tag is used to visualize cellular uptake.Incorporation of the non-viral cell-penetrating vector RRGRRG and R6 into the sequence doesnot alter its helical conformation, allowing efficient delivery of peptide carrier to the nucleus.The delivery is not effective for non-helical peptides. THP is stable against enzymaticdegradation, as studied in human serum. Because of its size and shape, the THP nanoparticlecarrier, a rigid rod with 1.5 nm diameter and adjustable length between 7.5 and 10 nm, has thepotential to be efficiently delivered to tumor cells via the Enhanced Permeation and Retention(EPR) effect. The ease of replacement of hydroxyproline with lysine during the synthesis of thepeptide allows for simple drug conjugation to the carrier and creates the potential for ligandattachments for targeted delivery.

Helical peptides for drug delivery applications

248th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.