A new class of promising drug carriers based on collagen mimetic peptides assembled into triple helical peptide (THP) is described. The peptides fold into a triple helical conformation forming high aspect ratio, rigid rod nanoparticles. The fluorescein tag is used to visualize cellular uptake. Incorporation of the non-viral cell-penetrating vector (RRG)2 and R6 into the sequence does not 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 enzymatic degradation, as studied in human serum. Because of its size and shape, the THP nanoparticle carrier, a rigid rod with 1.5 nm diameters and adjustable length between 7.5 and 10 nm, has the potential 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 the peptide allows for simple drug conjugation to the carrier.
|Commitee:||McAbee, Douglas, Narayanswami, Vasanthy|
|School:||California State University, Long Beach|
|Department:||Chemistry and Biochemistry|
|School Location:||United States -- California|
|Source:||MAI 52/01M(E), Masters Abstracts International|
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