Intracellular Delivery: Exploiting Viral Membranotropic Peptides (1011 views)
Current Drug Metabolism (ISSN: 1389-2002), 2012 Jan; 13(1): 93-104.
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Paper type: Journal Article,
Impact factor: 4.405, 5-year impact factor: 4.508
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84857613440&partnerID=40&md5=3d7b6495ae521ed3e192c152553d9fda
Keywords: Cell-Penetrating Peptides, Endocytosis, Intracellular Delivery, Membrane Fusion, Viral Fusion Proteins, Alamethicin, Arginine, Cell Penetrating Peptide, Clathrin, Coat Protein, Coat Protein Gamma Peptide, Drug Vehicle, Galanin, Gh625 Protein, Glycoprotein, Glycoprotein Gp 41, Hepatitis B Surface Antigen, Lysine, Mastoparan, Melittin, Membrane Protein, Model Amphipathic Peptide, Pep 1 Protein, Polyarginine, Polypeptide Antibiotic Agent, Pres2 Protein, Protein Vp22, Synthetic Peptide, Transactivator Protein, Transportan, Tryptophan, Unclassified Drug, Unindexed Drug, Virus Fusion Protein, Virus Protein, Amino Acid Sequence, Amino Acid Substitution, Cell Membrane Permeability, Cell Transport, Cytoplasm, Drug Delivery System, Drug Stability, Hepatitis B Virus, Herpes Simplex Virus 1, Human, Human Immunodeficiency Virus 1, Hydrophilicity, Hydrophobicity, Immunogenicity, Internalization, Nodavirus, Nonhuman, Nuclear Magnetic Resonance Spectroscopy, Protein Binding, Protein Conformation, Protein Domain, Protein Function, Protein Modification, Protein Motif, Protein Synthesis, Review, Signal Transduction, Thermodynamics, Virus Capsid, Virus Envelope, Virus Genome, Virus Replication, Virus Strain, Biological Transport, Cell Nucleus, Recombinant Fusion Proteins, Viral Proteins,
Affiliations:
*** IBB - CNR ***
Department of Experimental Medicine - II, University of Naples, Via De Crecchio 7, 80138, Napoli, Italy
Department of Biological Sciences, Division of Biostructures, University of Naples Federico II, Via Mezzocannone 16, 80134, Napoli, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Via Mezzocannone 16, 80134, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy
References:
Not available.
Current Drug Metabolism (ISSN: 1389-2002), 2012 Jan; 13(1): 93-104.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.405, 5-year impact factor: 4.508
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84857613440&partnerID=40&md5=3d7b6495ae521ed3e192c152553d9fda
Keywords: Cell-Penetrating Peptides, Endocytosis, Intracellular Delivery, Membrane Fusion, Viral Fusion Proteins, Alamethicin, Arginine, Cell Penetrating Peptide, Clathrin, Coat Protein, Coat Protein Gamma Peptide, Drug Vehicle, Galanin, Gh625 Protein, Glycoprotein, Glycoprotein Gp 41, Hepatitis B Surface Antigen, Lysine, Mastoparan, Melittin, Membrane Protein, Model Amphipathic Peptide, Pep 1 Protein, Polyarginine, Polypeptide Antibiotic Agent, Pres2 Protein, Protein Vp22, Synthetic Peptide, Transactivator Protein, Transportan, Tryptophan, Unclassified Drug, Unindexed Drug, Virus Fusion Protein, Virus Protein, Amino Acid Sequence, Amino Acid Substitution, Cell Membrane Permeability, Cell Transport, Cytoplasm, Drug Delivery System, Drug Stability, Hepatitis B Virus, Herpes Simplex Virus 1, Human, Human Immunodeficiency Virus 1, Hydrophilicity, Hydrophobicity, Immunogenicity, Internalization, Nodavirus, Nonhuman, Nuclear Magnetic Resonance Spectroscopy, Protein Binding, Protein Conformation, Protein Domain, Protein Function, Protein Modification, Protein Motif, Protein Synthesis, Review, Signal Transduction, Thermodynamics, Virus Capsid, Virus Envelope, Virus Genome, Virus Replication, Virus Strain, Biological Transport, Cell Nucleus, Recombinant Fusion Proteins, Viral Proteins,
Affiliations:
*** IBB - CNR ***
Department of Experimental Medicine - II, University of Naples, Via De Crecchio 7, 80138, Napoli, Italy
Department of Biological Sciences, Division of Biostructures, University of Naples Federico II, Via Mezzocannone 16, 80134, Napoli, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Via Mezzocannone 16, 80134, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy
References:
Not available.
Intracellular Delivery: Exploiting Viral Membranotropic Peptides
Recent advances in the understanding of cellular and molecular mechanisms of the pathogenesis of several diseases offer the possibility to address novel molecular targets for an improved diagnosis and therapy. In fact, in order to fulfill their function, macromolecular drugs, reporter molecules, and imaging agents often require to be delivered into specific intracellular compartments, usually the cytoplasm or the nucleus. From a medical perspective, biological membranes represent a critical hindrance due to their barrier-like behaviour not easily circumvented by many pharmacologically-active molecules. Therefore, identifying strategies for membrane translocation is essential. Several technologies have been designed to improve cellular uptake of therapeutic molecules, including cell-penetrating peptides (CPPs). These peptides, which are able to efficiently translocate macromolecules through the plasma membrane, have attracted a lot of attention, and new translocating peptides are continuously described. In this review, we will focus on the viral derived peptides, and in particular those derived by viral entry proteins that may be useful as delivery vehicles due to their intrinsic properties of inducing membrane perturbation. 2012 Bentham Science Publishers
Recent advances in the understanding of cellular and molecular mechanisms of the pathogenesis of several diseases offer the possibility to address novel molecular targets for an improved diagnosis and therapy. In fact, in order to fulfill their function, macromolecular drugs, reporter molecules, and imaging agents often require to be delivered into specific intracellular compartments, usually the cytoplasm or the nucleus. From a medical perspective, biological membranes represent a critical hindrance due to their barrier-like behaviour not easily circumvented by many pharmacologically-active molecules. Therefore, identifying strategies for membrane translocation is essential. Several technologies have been designed to improve cellular uptake of therapeutic molecules, including cell-penetrating peptides (CPPs). These peptides, which are able to efficiently translocate macromolecules through the plasma membrane, have attracted a lot of attention, and new translocating peptides are continuously described. In this review, we will focus on the viral derived peptides, and in particular those derived by viral entry proteins that may be useful as delivery vehicles due to their intrinsic properties of inducing membrane perturbation. 2012 Bentham Science Publishers
Intracellular Delivery: Exploiting Viral Membranotropic Peptides
| ▼ Targeting Sam-Sam interactions mediated by EphA2 receptor: design and evaluation of peptide inhibitors |
| ▼ Analysis of Sam domain druggability through computational and experimental studies |
Intracellular Delivery: Exploiting Viral Membranotropic Peptides
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Impact Factor: 1.951
View Export to BibTeX Export to EndNote
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* Membranotropic peptide-functionalized poly(lactide)- graft -poly(ethylene glycol) brush copolymers for intracellular delivery (445 views)
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Impact Factor: 5.554
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello M, Grieco P, Caraglia M, Morelli G, Galdiero M
* Exploitation of viral properties for intracellular delivery (526 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617linking), 2014 Jul; 20(7): 468-478.
Impact Factor: 1.546
View Export to BibTeX Export to EndNote
Accardo A, Aloj L, Aurilio M, Morelli G, Tesauro D
* Receptor binding peptides for target-selective delivery of nanoparticles encapsulated drugs (819 views)
Int J Nanomed (ISSN: 1178-2013, 1176-9114, 1176-9114linking), 2014 Mar 27; 9(1): 1537-1557.
Impact Factor: 4.383
View Export to BibTeX Export to EndNote
Cantisani M, Falanga A, Incoronato N, Russo L, De Simone A, Morelli G, Berisio R, Galdiero M, Galdiero S
* Conformational modifications of gB from herpes simplex virus type 1 analyzed by synthetic peptides (758 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2013 Nov 14; 56(21): 8366-8376.
Impact Factor: 5.48
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Tarallo R, Russo L, Galdiero E, Cantisani M, Morelli G, Galdiero M
* Peptide inhibitors against herpes simplex virus infections (1266 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Mar; 19(3): 148-158.
Impact Factor: 1.862
View Export to BibTeX Export to EndNote
Smaldone G, Falanga A, Capasso D, Guarnieri D, Correale S, Galdiero M, Netti PA, Zollo M, Galdiero S, Di Gaetano S, Pedone E
* 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.
Impact Factor: 4.195
View Export to BibTeX Export to EndNote
Galdiero S, Russo L, Falanga A, Cantisani M, Vitiello M, Fattorusso R, Malgieri G, Galdiero M, Isernia C
* Structure and Orientation of the gH625-644 Membrane Interacting Region of Herpes Simplex Virus Type 1 in a Membrane Mimetic System (416 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2012 Apr 10; 51(14): 3121-3128.
Impact Factor: 3.377
View Export to BibTeX Export to EndNote
Mercurio FA, Marasco D, Pirone L, Pedone E, Pellecchia M, Leone M
* Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 Receptor (475 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2012 Mar 13; 51(10): 2136-2145.
Impact Factor: 3.377
View Export to BibTeX Export to EndNote
Merlino A, Vitiello G, Grimaldi M, Sica F, Busi E, Basosi R, D’Ursi A, Fragneto G, Paduano L, D’Errico G
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J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2012 Jan 12; 116(1): 401-412.
Impact Factor: 3.607
View Export to BibTeX Export to EndNote
Falanga A, Vitiello MT, Cantisani M, Tarallo R, Guarnieri D, Mignogna E, Netti P, Pedone C, Galdiero M, Galdiero S
* A peptide derived from herpes simplex virus type 1 glycoprotein H: membrane translocation and applications to the delivery of quantum dots (1215 views)
Nanomedicine (ISSN: 1549-9642, 1549-9634, 1549-9642electronic), 2011 Dec; 7(6): 925-934.
Impact Factor: 6.692
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello M, Raiola L, Russo L, Pedone C, Isernia C, Galdiero M
* The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein (480 views)
Jbc Papers (ISSN: 1083-351x, 0021-9258, 0021-9258linking), 2010 May 28; 285(22): 17123-17136.
Impact Factor: 5.328
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello G, Vitiello M, Pedone C, D'Errico G, Galdiero M
* Role of membranotropic sequences from herpes simplex virus type I glycoproteins B and H in the fusion process (578 views)
Bba-Gen Subjects (ISSN: 0006-3002, 0005-2736, 0925-4439), 2010 Mar; 1798(3): 579-591.
Impact Factor: 4.647
View Export to BibTeX Export to EndNote
Vitiello M, Finamore E, Falanga A, Raieta K, Cantisani M, Galdiero F, Pedone C, Galdiero M, Galdiero S
* Viral fusion peptides induce several signal transduction pathway activations that are essential for interleukin-10 and beta-interferon production (483 views)
Intervirology (ISSN: 1423-0100, 0300-5526), 2010; 53(6): 381-389.
Impact Factor: 1.756
View Export to BibTeX Export to EndNote
Falanga A, Cantisani M, Pedone C, Galdiero S
* Membrane fusion and fission: enveloped viruses (454 views)
Protein Pept Lett (ISSN: 1875-5305, 0929-8665), 2009 Jul; 16(7): 751-759.
Impact Factor: 1.755
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello M, Raiola L, Fattorusso R, Browne H, Pedone C, Isernia C, Galdiero M
* Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein (650 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 31; 283(44): 29993-30009.
Impact Factor: 5.52
View Export to BibTeX Export to EndNote
Galdiero S, Vitiello M, Falanga A, D'Isanto M, Cantisani M, Kampanaraki A, Benedetti E, Browne H, Galdiero M
* Peptides containing membrane-interacting motifs inhibit herpes simplex virus type 1 infectivity (481 views)
Peptides (ISSN: 0196-9781, 1873-5169electronic, 0196-9781linking), 2008 Sep; 29(9): 1461-1471.
Impact Factor: 2.565
View Export to BibTeX Export to EndNote
Galdiero S, Vitiello M, D'Isanto M, Falanga A, Cantisani M, Browne H, Pedone C, Galdiero M
* The identification and characterization of fusogenic domains in herpes virus glycoprotein B molecules (542 views)
Chembiochem (ISSN: 1439-7633, 1439-4227, 1439-7633electronic), 2008 Mar 25; 9(5): 758-767.
Impact Factor: 3.322
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello M, D'Isanto M, Collins C, Orrei V, Browne H, Pedone C, Galdiero M
* Evidence for a role of the membrane-proximal region of herpes simplex virus type 1 glycoprotein H in membrane fusion and virus inhibition (639 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2007 May 25; 8(8): 885-895.
Impact Factor: 3.446
View Export to BibTeX Export to EndNote
Galdiero S, Vitiello M, D'Isanto M, Falanga A, Collins C, Raieta K, Pedone C, Browne H, Galdiero M
* Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and (662 views)
Journal Of General Virology (ISSN: 0022-1317), 2006 May; 87: 1085-1097.
Impact Factor: 3.11
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello M, Browne H, Pedone C, Galdiero M
* Fusogenic domains in herpes simplex virus type 1 glycoprotein (598 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Sep 5; 280(31): 28632-28643.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Vitiello M, Finamore E, Falanga A, Raieta K, Cantisani M, Galdiero F, Pedone C, Galdiero M, Galdiero S
* Fusion in Coq (512 views)
Lecture Notes In Computer Science (ISSN: 0302-9743, 0302-974335404636319783540463634, 0302-974335402975459783540297543), 2001; 2178LNCS: 583-596.
Impact Factor: 0.415
View Export to BibTeX Export to EndNote
Trischitta V, Wong KY, Brunetti A, Scalisi R, Vigneri R, Goldfine ID
Endocytosis, recycling, and degradation of the insulin receptor. Studies with monoclonal antireceptor antibodies that do not activate receptor kinase (317 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 1989 Mar 25; 264(9): 5041-5046.
Impact Factor: 6.963
View Export to BibTeX Export to EndNote
25 Records (24 excluding Abstracts).
Total impact factor: 89.939 (86.705 excluding Abstracts).
Total 5 year impact factor: 88.994 (85.292 excluding Abstracts).
Total impact factor: 89.939 (86.705 excluding Abstracts).
Total 5 year impact factor: 88.994 (85.292 excluding Abstracts).
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