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• W2078204057 endingPage "247" @default.
• W2078204057 startingPage "231" @default.
• W2078204057 abstract "The incorporation of pegylated lipid into Lipid-Protamine-DNA (LPD-PEG) lipopolyplexes causes a decrease of their in vitro transfection activity. This can be partially attributed to a reduction in particle binding to cells. To restore particle binding and specifically target LPD formulations to tumor cells, the lipid-peptide conjugate DSPE-PEG5K-succinyl-ACDCRGDCFCG-COOH (DSPE-PEG5K-RGD-4C) was generated and incorporated into LPD formulations (LPD-PEG-RGD). LPD-PEG-RGD was characterized with respect to its biophysical and biological properties. The Incorporation of DSPE-PEG5K-RGD-4C ligands into LPD formulations results in a 5 and a 15 fold increase in the LPD-PEG-RGD binding and uptake, respectively, over an LPD-PEG formulation. Enhancement of binding and uptake resulted in a 100 fold enhancement of transfection activity. Moreover, this transfection enhancement was specific to cells expressing appropriate integrin receptors (MDA-MB-231). Huh7 cells, known for their low level of alphavbeta3 and alphavbeta5 integrin expression, failed to show RGD mediated transfection enhancement. This transfection enhancement can be abolished in a competitive manner using free RGD peptide, but not an RGE control peptide. Results demonstrated RGD mediated enhanced LPD-PEG cell binding and transfection in cells expressing the integrin receptor. These formulations provide the basis for effective, targeted, systemic gene delivery." @default.
• W2078204057 created "2016-06-24" @default.
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• W2078204057 date "2003-01-01" @default.
• W2078204057 modified "2023-09-24" @default.
• W2078204057 title "Targeting of Lipid-Protamine-DNA (LPD) Lipopolyplexes Using RGD Motifs" @default.
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• W2078204057 doi "https://doi.org/10.1081/lpr-120026389" @default.
• W2078204057 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14670229" @default.
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