Journal
BIOCHEMISTRY
Volume 48, Issue 15, Pages 3304-3314Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi802356k
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Funding
- National Heart, Lung and Blood Institute Grant [5 U54 CAI 19335-04]
- MRSEC Program of the National Science Foundation [DMR05-20415]
- Army Research Office through the Institute for Collaborative Biotechnologies
- NIH [P41RR02250]
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Self-assembly of peptide amphiphiles into nanostructures makes them attractive for a variety of applications in drug and peptide delivery. We here report on the interactions of micelles composed of a palmitoylated, pro-apoptotic peptide derived from p53 tumor suppressor protein with a human cancer cell line. Characterization of self-assembly in aqueous buffered solutions revealed formation of elongated rod-like micelles above a critical micelle concentration. Our results however demonstrate that monomers instead of micelles are internalized, a finding that correlates with the dynamic nature of the assemblies and the noncovalent interactions that hold them together. Internalization is shown to occur via adsorption-mediated, energy-dependent pathways, resulting in accumulation of the material in endocytic vesicles. We conclude that palmitoylation of peptides is an efficient way to increase peptide permeability inside SJSA-1 cells and that increased micelle stability would be required for intact micelle internalization.
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