Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4 (797 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2015; 16(6): 12159-12173.
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Paper type: Journal Article,
Impact factor: 3.257, 5-year impact factor: 3.213
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84930636141&partnerID=40&md5=3b2345c8b9e709bb01a096a4e4353606
Keywords: Chemokine, Conformational Ensemble, Intrinsically Disordered Protein (id), Intrinsically Disordered Region(idr), Chemokine Receptor Cxcr4, Antigen Binding, Article, Binding Assay, Camp Assay, Cell Migration Assay, Circular Dichroism, Controlled Study, Human, Human Cell, Hydrogen Bond, Mass Spectrometry, Molecular Dynamics, Molecular Recognition, Nuclear Magnetic Resonance Spectroscopy, Peptide Synthesis, Protein Conformation, Receptor Binding, Reversed Phase High Performance Liquid Chromatography, Simulation,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, University of Naples “Federico II” and CIRPeB, Via Mezzocannone 16, Naples, Italy
Institute of Biostructures and Bioimaging (IBB), National Research Council (CNR), Via Mezzocannone 16, Naples, Italy
Oncology Research Center of Mercogliano (CROM), Istituto Nazionale Tumori “Fondazione G. Pascale”, IRCCS, Napoli, Italy
Molecular Immunology and Immuneregulation, Istituto Nazionale Tumori “Fondazione G. Pascale”, IRCCS, Napoli, Italy
Center of Medical Informatics, AOU Second University of Naples, Napoli, Italy
UFR des Sciences Pharmaceutiques—Collège Sciences de la Santé INSERM U869, Laboratoire ARNA, Université de Bordeaux, 146 rue Léo Saignat, Bordeaux cedex, France
References:
Not available.
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2015; 16(6): 12159-12173.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.257, 5-year impact factor: 3.213
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84930636141&partnerID=40&md5=3b2345c8b9e709bb01a096a4e4353606
Keywords: Chemokine, Conformational Ensemble, Intrinsically Disordered Protein (id), Intrinsically Disordered Region(idr), Chemokine Receptor Cxcr4, Antigen Binding, Article, Binding Assay, Camp Assay, Cell Migration Assay, Circular Dichroism, Controlled Study, Human, Human Cell, Hydrogen Bond, Mass Spectrometry, Molecular Dynamics, Molecular Recognition, Nuclear Magnetic Resonance Spectroscopy, Peptide Synthesis, Protein Conformation, Receptor Binding, Reversed Phase High Performance Liquid Chromatography, Simulation,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, University of Naples “Federico II” and CIRPeB, Via Mezzocannone 16, Naples, Italy
Institute of Biostructures and Bioimaging (IBB), National Research Council (CNR), Via Mezzocannone 16, Naples, Italy
Oncology Research Center of Mercogliano (CROM), Istituto Nazionale Tumori “Fondazione G. Pascale”, IRCCS, Napoli, Italy
Molecular Immunology and Immuneregulation, Istituto Nazionale Tumori “Fondazione G. Pascale”, IRCCS, Napoli, Italy
Center of Medical Informatics, AOU Second University of Naples, Napoli, Italy
UFR des Sciences Pharmaceutiques—Collège Sciences de la Santé INSERM U869, Laboratoire ARNA, Université de Bordeaux, 146 rue Léo Saignat, Bordeaux cedex, France
References:
Not available.
Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4
This work reports on the design andthe synthesis of two short linear peptides both containing a few amino acids with disorder propensity and an allylic ester group at the C-terminal end. Their structural properties were firstly analyzed by means of experimental techniques in solution such as CD and NMR methodsthat highlighted peptide flexibility. These results were further confirmed by MD simulationsthat demonstrated the ability of the peptides to assume conformational ensembles. Theyrevealed a network of transient and dynamic -bonds and interactions with water molecules. Binding assays with a well-known drug-target, i.e., the CXCR4 receptor, were also carried out in an attempt to verify their biological function and the possibility to use the assays to develop new specific targets for CXCR4. Moreover, our data indicate that these peptides represent useful tools for molecular recognition processes in which a flexible conformation is required in order to obtain an interaction with a specific target. © 2015 by the authors; licensee MDPI, Basel, Switzerland.
This work reports on the design andthe synthesis of two short linear peptides both containing a few amino acids with disorder propensity and an allylic ester group at the C-terminal end. Their structural properties were firstly analyzed by means of experimental techniques in solution such as CD and NMR methodsthat highlighted peptide flexibility. These results were further confirmed by MD simulationsthat demonstrated the ability of the peptides to assume conformational ensembles. Theyrevealed a network of transient and dynamic -bonds and interactions with water molecules. Binding assays with a well-known drug-target, i.e., the CXCR4 receptor, were also carried out in an attempt to verify their biological function and the possibility to use the assays to develop new specific targets for CXCR4. Moreover, our data indicate that these peptides represent useful tools for molecular recognition processes in which a flexible conformation is required in order to obtain an interaction with a specific target. © 2015 by the authors; licensee MDPI, Basel, Switzerland.
Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4
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Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4
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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: 3.415
View Export to BibTeX Export to EndNote
Verdoliva A, Marasco D, De Capua A, Saporito A, Bellofiore P, Manfredi V, Fattorusso R, Pedone C, Ruvo M
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Impact Factor: 3.94
View Export to BibTeX Export to EndNote
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* A simplified model of the binding interaction between stromal cell-derived factor-1 chemokine and CXC chemokine receptor (461 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2003 Apr; 10(2): 133-138.
Impact Factor: 0.46
View Export to BibTeX Export to EndNote
Palladino P, De Capua A, Pedone C, Ragone R, Rossi F, Limatola C, Ragozzino D, Benedetti E
* A simplified model of the interaction between SDF-1 chemokine and the CXCR4 receptor (620 views)
Peptide Revolution, 2003 Apr; 10(2): 133-138.
Impact Factor: 4.659
View Export to BibTeX Export to EndNote
19 Records (18 excluding Abstracts).
Total impact factor: 72.139 (68.605 excluding Abstracts).
Total 5 year impact factor: 67.217 (63.202 excluding Abstracts).
Total impact factor: 72.139 (68.605 excluding Abstracts).
Total 5 year impact factor: 67.217 (63.202 excluding Abstracts).
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