http://www.cnr.it/ontology/cnr/individuo/prodotto/ID307492
gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins (Articolo in rivista)
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- gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.2147/IJN.S44186 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Smaldone G.; Falanga A.; Capasso D.; Guarnieri D.; Correale S.; Galdiero M.; Netti P.A.; Zollo M.; Galdiero S.; Di Gaetano S.; Pedone E. (literal)
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- http://www.scopus.com/inward/record.url?eid=2-s2.0-84884186694&partnerID=q2rCbXpz (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
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- Institute of Biostructures and Bioimaging, National Research Council, Naples, Italy; Department of Pharmacy and Interuniversity Research Center on Bioactive Peptides, Federico II University of Naples, Naples, Italy; Molecular Diagnostics and Pharmaceuticals Scarl, Naples, Italy; Special Center for Biotechnology, Federico II University of Naples, Naples, Italy; Center for Advanced Biomaterials for Health Care, Interdisciplinary Research Centre on Biomaterials, Italian Institute of Technology, Naples, Italy; Interdisciplinary Research Centre on Biomaterials, Federico II University of Naples, Naples, Italy; Kedrion S.p.A, Sant'Antimo, Naples, Italy; Department of Experimental Medicine, Federico II University of Naples, Naples, Italy; CEINGE - Advanced Biotechnology Scarl, Naples, Italy (literal)
- Titolo
- gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins (literal)
- Abstract
- 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. © 2013 Smaldone et al, publisher and licensee Dove Medical Press Ltd. (literal)
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