A peptide derived from herpes simplex virus type 1 glycoprotein H: membrane translocation and applications to the delivery of quantum dots

Falanga, Annarita; Vitiello, Maria Teresa; Cantisani, Marco; Tarallo, Rossella; Guarnieri, Daniela; Mignogna, Eleonora; Netti, Paolo A.; Pedone, Carlo; Galdiero, Massimiliano; Galdiero, Stefania

doi:10.1016/j.nano.2011.04.009

Cited by 75 publications

(85 citation statements)

References 43 publications

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“…We recently reported about the functionalization of CdSe QDs with gH625, which enhanced their uptake essentially involving nonendocytic pathways. 20 The novelty and complexity of this subject together with the lack of homogeneity in the kind of NPs and methods to analyze the complex interactions with living systems make it difficult to provide standardized information on toxicity.…”

Section: Introductionmentioning

confidence: 99%

Daphnia magna and Xenopus laevis as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

Galdiero¹,

Falanga²,

Siciliano³

et al. 2017

IJN

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The use of quantum dots (QDs) for nanomedicine is hampered by their potential toxicologic effects and difficulties with delivery into the cell interior. We accomplished an in vivo study exploiting Daphnia magna and Xenopus laevis to evaluate both toxicity and uptake of QDs coated with the membranotropic peptide gH625 derived from the glycoprotein H of herpes simplex virus and widely used for drug delivery studies. We evaluated and compared the effects of QDs and gH625-QDs on the survival, uptake, induction of several responsive pathways and genotoxicity in D. magna , and we found that QDs coating plays a key role. Moreover, studies on X. laevis embryos allowed to better understand their cell/tissue localization and delivery efficacy. X. laevis embryos raised in Frog Embryo Teratogenesis Assay- Xenopus containing QDs or gH625-QDs showed that both nanoparticles localized in the gills, lung and intestine, but they showed different distributions, indicating that the uptake of gH625-QDs was enhanced; the functionalized QDs had a significantly lower toxic effect on embryos’ survival and phenotypes. We observed that D. magna and X. laevis are useful in vivo models for toxicity and drug delivery studies.

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Section: Introductionmentioning

confidence: 99%

Daphnia magna and Xenopus laevis as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

Galdiero¹,

Falanga²,

Siciliano³

et al. 2017

IJN

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“…The presence of advanced technologies for peptide identification and modification further supports the extensive application of peptides in the field of theranostics research. 31,32 We have previously demonstrated that gH625, a 19-residue peptide, is a membrane-perturbing domain 13 that interacts with model membranes, contributing to their merging 13 and is able to traverse the membrane bilayer and transport a cargo (quantum dots, liposomes, and dendrimers) 16,18,20 into the cytoplasm and across an in vitro model of the BBB. 19 Uptake studies suggested a nonactive translocation mechanism in crossing the lipid bilayer, which may vary depending on the cargo.…”

Section: Discussionmentioning

confidence: 99%

“…15 Further, gH625 has been used extensively for vector-mediated strategies that enable passage of a large variety of small molecules as well as proteins across cell membranes in vitro. [16][17][18][19][20] Conjugation of gH625 to the surface of nanoparticles also enhances their transport across the BBB, as previously demonstrated in an in vitro model of the BBB. 19 Whether or not multifunctional nanodevices, designed and tested in vitro, work properly in vivo in a mammalian host is still not fully understood.…”

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confidence: 97%

Peptide gH625 enters into neuron and astrocyte cell lines and crosses the blood–brain barrier in rats

Valiante¹,

Falanga²,

Cigliano³

et al. 2015

IJN

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Peptide gH625, derived from glycoprotein H of herpes simplex virus type 1, can enter cells efficiently and deliver a cargo. Nanoparticles armed with gH625 are able to cross an in vitro model of the blood–brain barrier (BBB). In the present study, in vitro experiments were performed to investigate whether gH625 can enter and accumulate in neuron and astrocyte cell lines. The ability of gH625 to cross the BBB in vivo was also evaluated. gH625 was administered in vivo to rats and its presence in the liver and in the brain was detected. Within 3.5 hours of intravenous administration, gH625 can be found beyond the BBB in proximity to cell neurites. gH625 has no toxic effects in vivo, since it does not affect the maximal oxidative capacity of the brain or the mitochondrial respiration rate. Our data suggest that gH625, with its ability to cross the BBB, represents a novel nanocarrier system for drug delivery to the central nervous system. These results open up new possibilities for direct delivery of drugs into patients in the field of theranostics and might address the treatment of several human diseases.

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“…1,2,17,18 In particular, we recently reported the ability of gH625 peptide to transport quantum dots inside the cytoplasm in an efficient way and only partially involving endocytic pathways; 18 moreover, we reported its ability to enhance intracellular penetration of liposomes functionalized with the peptide on the external leaflet, 17 nanoparticles, 2 and dendrimers. 19 Compared with the TAT peptide, which mainly exploits the endocytic pathway, the viral membranotropic peptide gH625 crosses membrane bilayers mainly through a translocation mechanism.…”

Section: Introductionmentioning

confidence: 93%

gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins

Smaldone¹,

Falanga²,

Capasso³

et al. 2013

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A genetically modified recombinant gH625-c-prune was prepared through conjugation of c-prune with gH625, a peptide encompassing 625-644 residues of the glycoprotein H of herpes simplex virus 1, which has been proved to possess the ability to carry cargo molecules across cell membranes. C-prune is the C-terminal domain of h-prune, overexpressed in breast, colorectal, and gastric cancers, interacting with multiple partners, and representing an ideal target for inhibition of cancer development. Its C-terminal domain results in an intrinsically disordered domain (IDD), and the peculiar properties of gH625 render it an optimal candidate to act as a carrier for this net negatively charged molecule by comparison with the positively charged TAT. A characterization of the recombinant gH625-c-prune fusion protein was conducted by biochemical, cellular biology and confocal microscopy means in comparison with TAT-c-prune. The results showed that the gH625-c-prune exhibited the ability to cross biomembranes, opening a new scenario on the use of gH625 as a novel multifunctional carrier.

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A peptide derived from herpes simplex virus type 1 glycoprotein H: membrane translocation and applications to the delivery of quantum dots

Cited by 75 publications

References 43 publications

<em>Daphnia magna</em> and<em> Xenopus laevis</em> as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

<em>Daphnia magna</em> and<em> Xenopus laevis</em> as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

Peptide gH625 enters into neuron and astrocyte cell lines and crosses the blood–brain barrier in rats

gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins

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A peptide derived from herpes simplex virus type 1 glycoprotein H: membrane translocation and applications to the delivery of quantum dots

Cited by 75 publications

References 43 publications

<em>Daphnia magna</em> and<em> Xenopus laevis</em> as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

<em>Daphnia magna</em> and<em> Xenopus laevis</em> as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

Peptide gH625 enters into neuron and astrocyte cell lines and crosses the blood&ndash;brain barrier in&nbsp;rats

gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins

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Peptide gH625 enters into neuron and astrocyte cell lines and crosses the blood–brain barrier in rats