gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins (463 views)
Int J Nanomed (ISSN: 1178-2013, 1176-9114, 1178-2013electronic), 2013; 8: 2555-2565.
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Paper type: Journal Article,
Impact factor: 4.195, 5-year impact factor: 4.53
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84884186694&partnerID=40&md5=53bf2e1bfe4bfb87866fcbd0a8498862
Keywords: Delivery, Cell Penetrating Peptide, Drug Carrier, Gh625 C Prune, Tat C Prune, Transactivator Protein, Unclassified Drug, Virus Glycoprotein, Article, Carboxy Terminal Sequence, Cell Membrane Permeability, Confocal Microscopy, Controlled Study, Drug Conjugation, Drug Delivery System, Drug Mixture, Herpes Simplex Virus 1, Human, Human Cell, Nonhuman, Surface Charge, Carrier Proteins, Circular Dichroism, Endocytosis, Hela Cells, Intrinsically Disordered Proteins, Neoplasm Proteins, Protein Structure, Tertiary, Recombinant Fusion Proteins, Viral Envelope Proteins,
Affiliations:
*** IBB - CNR ***
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
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
Kedrion S. p. A, Sant'Antimo, Naples, Italy
References:
Not available.
Int J Nanomed (ISSN: 1178-2013, 1176-9114, 1178-2013electronic), 2013; 8: 2555-2565.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.195, 5-year impact factor: 4.53
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84884186694&partnerID=40&md5=53bf2e1bfe4bfb87866fcbd0a8498862
Keywords: Delivery, Cell Penetrating Peptide, Drug Carrier, Gh625 C Prune, Tat C Prune, Transactivator Protein, Unclassified Drug, Virus Glycoprotein, Article, Carboxy Terminal Sequence, Cell Membrane Permeability, Confocal Microscopy, Controlled Study, Drug Conjugation, Drug Delivery System, Drug Mixture, Herpes Simplex Virus 1, Human, Human Cell, Nonhuman, Surface Charge, Carrier Proteins, Circular Dichroism, Endocytosis, Hela Cells, Intrinsically Disordered Proteins, Neoplasm Proteins, Protein Structure, Tertiary, Recombinant Fusion Proteins, Viral Envelope Proteins,
Affiliations:
*** IBB - CNR ***
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
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
Kedrion S. p. A, Sant'Antimo, Naples, Italy
References:
Not available.
gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins
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.
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.
gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins
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gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 3.15
View Export to BibTeX Export to EndNote
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Impact Factor: 2.389
View Export to BibTeX Export to EndNote
Cortesi R, Mischiati C, Borgatti M, Breda L, Romanelli A, Saviano M, Pedone C, Gambari R, Nastruzzi C
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Impact Factor: 1.938
View Export to BibTeX Export to EndNote
Esposito G, Ligresti A, Izzo AA, Bisogno T, Ruvo M, Di Rosa M, Di Marzo V, Iuvone T
* The endocannabinoid system protects rat glioma cells against HIV-1 Tat protein-induced cytotoxicity: Mechanism and regulation (608 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2002 Dec 27; 277(52): 50348-50354.
Impact Factor: 6.696
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29 Records (25 excluding Abstracts).
Total impact factor: 90.758 (81.907 excluding Abstracts).
Total 5 year impact factor: 96.825 (83.343 excluding Abstracts).
Total impact factor: 90.758 (81.907 excluding Abstracts).
Total 5 year impact factor: 96.825 (83.343 excluding Abstracts).
463 views. Last view on Tuesday 29 August 2023, 3:55:32
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