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Amphiphilic Polypeptoids Rupture Vesicle Bilayers To Form Peptoid–Lipid Fragments Effective in Enhancing Hydrophobic Drug Delivery

Journal Article · · Langmuir

Peptoids are highly biocompatible pseudopeptidic polyglycines with designable substituents on the nitrogen atoms. The therapeutic and drug-carrying potential of these materials requires a fundamental understanding of their interactions with lipid bilayers. Here, we use amphiphilic polypeptoids with up to 100 monomeric units where a significant fraction (26%) of the nitrogen atoms are functionalized with decyl groups (hydrophobes) that insert into the lipid bilayer through the hydrophobic effect. These hydrophobically modified polypeptoids (HMPs) insert their hydrophobes into lipid bilayers creating instabilities that lead to the rupture of vesicles. At low HMP concentrations, such rupture leads to the creation of large fragments which remarkably anchor to intact vesicles through the hydrophobic effect. At high HMP concentrations, all vesicles rupture to smaller HMP–lipid fragments of the order of 10 nm. We show that the technique for such nanoscale polymer–lipid fragments can be exploited to sustain highly hydrophobic drug species in solution. Using the kinase inhibitor, Sorafenib as a model drug, it is shown that HMP–lipid fragments containing the drug can efficiently enter a hepatocellular carcinoma cell line (Huh 7.5), indicating the use of such fragments as drug delivery nanocarriers.

Research Organization:
Louisiana State Univ., Baton Rouge, LA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); National Science Foundation (NSF)
Grant/Contract Number:
SC0012432
OSTI ID:
1615947
Alternate ID(s):
OSTI ID: 1672152
Journal Information:
Langmuir, Journal Name: Langmuir Journal Issue: 47 Vol. 35; ISSN 0743-7463
Publisher:
American Chemical SocietyCopyright Statement
Country of Publication:
United States
Language:
English

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