2013
DOI: 10.2217/nnm.12.201
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Modified Dipeptide-Based Nanoparticles: Vehicles for Targeted Tumor Drug Delivery

Abstract: Arg-α,β-dehydrophenylalanine formed self-assembled nanoparticles that could be easily derivatized with folic acid. Folic acid-derivatized nanoparticles showed enhanced cellular uptake and, when loaded with doxorubicin, showed enhanced tumor regression compared with underivatized nanoparticles or native drug, without any adverse side effects, both in vitro and in vivo.

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Cited by 33 publications
(38 citation statements)
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“…Loading capacity of, and the release of miRNA from its complex with RΔF‐LA NPs indicated their suitability as possible delivery agent for miRNA. The ability of any NPs based delivery systems to protect their cargos including oligonucleotides in in vivo enzymatic conditions is an important prerequisite parameter for their potential use in clinical applications . Results of stability experiment showed that miR‐199a‐3p was stable in serum as well as to the action of RNase A.…”
Section: Discussionmentioning
confidence: 99%
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“…Loading capacity of, and the release of miRNA from its complex with RΔF‐LA NPs indicated their suitability as possible delivery agent for miRNA. The ability of any NPs based delivery systems to protect their cargos including oligonucleotides in in vivo enzymatic conditions is an important prerequisite parameter for their potential use in clinical applications . Results of stability experiment showed that miR‐199a‐3p was stable in serum as well as to the action of RNase A.…”
Section: Discussionmentioning
confidence: 99%
“…Our study paves the way for future investigations using a large cohort of mice and testing a range of doses of RΔF‐LA/miR NPs for therapeutic potency. It may also be possible to deliver both miRNA and an anticancer drug simultaneously to the tumor site using this peptide based NPs …”
Section: Discussionmentioning
confidence: 99%
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“…Here, we report spontaneous self-assembly of a dipeptide, Leucine-α, β-dehydrophenylalanine, containing a non-protein amino acid, α,β-dehydrophenylalanine (ΔPhe) at its C-terminal, into a highly stable hydrogel under physiological conditions. ΔPhe is an analogue of phenylalanine, with a double bond between C α and C β atoms, whose incorporation in peptide sequences introduces conformational constraint in the peptide backbone and provides increased resistance to enzymatic degradation 8 9 10 . The hydrogel formed by LeuΔPhe was translucent, self-supportive, fractaline in nature, of high mechanical strength, non-toxic, injectable, proteolytically stable and responsive to external stimuli like ionic strength, pH and temperature.…”
mentioning
confidence: 99%
“…The spontaneous self-assembly of a dipeptide, Leucine-α,βdehydrophenylalanine, containing a non-protein amino acid, α,β-dehydrophenylalanine (ΔPhe) at its C-terminal, into a highly stable hydrogel under physiological conditions. ΔPhe is an analogue of phenylalanine, with a double bond between Cα and Cβ atoms, whose incorporation in peptide sequences introduces conformational restriction in the peptide backbone and provides increased resistance to enzymatic degradation [ 25 , 26 ]. The hydrogel designed by LeuΔPhe was transparent, self-supportive, fractaline in nature, of high mechanical strength, non-toxic, injectable, proteolytically stable and responsive to external stimuli, such as ionic strength, pH and temperature.…”
Section: Introductionmentioning
confidence: 99%