The Ionophoric Activity of a Pro-Apoptotic VEGF165 Fragment on HUVEC Cells
Copper plays an important role as a regulator in many pathologies involving the angiogenesis process. In cancerogenesis, tumor progression, and angiogenic diseases, copper homeostasis is altered. Although many details in the pathways involved are still unknown, some copper-specific ligands have been...
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| Veröffentlicht in: | International journal of molecular sciences 2020-04, Vol.21 (8), p.2866 |
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| creator | Zimbone, Stefania Santoro, Anna M La Mendola, Diego Giacomelli, Chiara Trincavelli, Maria L Tomasello, Marianna F Milardi, Danilo García-Viñuales, Sara Sciacca, Michele F M Martini, Claudia Grasso, Giulia |
| description | Copper plays an important role as a regulator in many pathologies involving the angiogenesis process. In cancerogenesis, tumor progression, and angiogenic diseases, copper homeostasis is altered. Although many details in the pathways involved are still unknown, some copper-specific ligands have been successfully used as therapeutic agents. Copper-binding peptides able to modulate angiogenesis represent a possible way to value new drugs. We previously reported that a fragment (VEGF73-101) of vascular endothelial growth factor (VEGF165), a potent angiogenic, induced an apoptotic effect on human umbilical vein endothelial cells. The aim of this study was to investigate the putative copper ionophoric activity of VEGF73-101, as well as establish a relationship between the structure of the peptide fragment and the cytotoxic activity in the presence of copper(II) ions. Here, we studied the stoichiometry and the conformation of the VEGF73-101/Cu(II) complexes and some of its mutated peptides by electrospray ionization mass spectrometry and circular dichroism spectroscopy. Furthermore, we evaluated the effect of all peptides in the absence and presence of copper ions by cell viability and cytofuorimetric assays. The obtained results suggest that VEGF73-101 could be considered an interesting candidate in the development of new molecules with ionophoric properties as agents in antiangiogenic therapeutic approaches. |
| doi_str_mv | 10.3390/ijms21082866 |
| format | Article |
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In cancerogenesis, tumor progression, and angiogenic diseases, copper homeostasis is altered. Although many details in the pathways involved are still unknown, some copper-specific ligands have been successfully used as therapeutic agents. Copper-binding peptides able to modulate angiogenesis represent a possible way to value new drugs. We previously reported that a fragment (VEGF73-101) of vascular endothelial growth factor (VEGF165), a potent angiogenic, induced an apoptotic effect on human umbilical vein endothelial cells. The aim of this study was to investigate the putative copper ionophoric activity of VEGF73-101, as well as establish a relationship between the structure of the peptide fragment and the cytotoxic activity in the presence of copper(II) ions. Here, we studied the stoichiometry and the conformation of the VEGF73-101/Cu(II) complexes and some of its mutated peptides by electrospray ionization mass spectrometry and circular dichroism spectroscopy. Furthermore, we evaluated the effect of all peptides in the absence and presence of copper ions by cell viability and cytofuorimetric assays. The obtained results suggest that VEGF73-101 could be considered an interesting candidate in the development of new molecules with ionophoric properties as agents in antiangiogenic therapeutic approaches.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms21082866</identifier><identifier>PMID: 32325956</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino Acid Sequence ; Amino acids ; Angiogenesis ; Antiangiogenics ; Apoptosis ; Apoptosis - drug effects ; Apoptosis - genetics ; Cell Membrane Permeability ; Cell Survival - drug effects ; Cell viability ; Chelating Agents - pharmacology ; Chemical compounds ; Chromatography ; Circular dichroism ; Conformation ; Copper - metabolism ; Copper compounds ; Cytotoxicity ; Dichroism ; Endothelial cells ; Growth factors ; Homeostasis ; Human Umbilical Vein Endothelial Cells - metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Kinases ; Ligands ; Mass spectrometry ; Mass spectroscopy ; Mutation ; Neovascularization, Physiologic - drug effects ; Neovascularization, Physiologic - genetics ; Peptide Fragments - chemistry ; Peptide Fragments - pharmacology ; Peptides ; Permeability ; Pharmacology ; Protein Binding ; Protein Conformation ; Retention ; Spectrometry, Mass, Electrospray Ionization ; Spectrum Analysis ; Stoichiometry ; Structure-Activity Relationship ; Umbilical vein ; Vascular endothelial growth factor ; Vascular Endothelial Growth Factor A - chemistry ; Vascular Endothelial Growth Factor A - genetics ; Vascular Endothelial Growth Factor A - metabolism ; Vascular Endothelial Growth Factor A - pharmacology</subject><ispartof>International journal of molecular sciences, 2020-04, Vol.21 (8), p.2866</ispartof><rights>2020. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2020 by the authors. 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-baf3c3f41f7a5861c8ab33c0a8a9e4c73d5241cc9af56ccf7633586f03380a103</citedby><cites>FETCH-LOGICAL-c412t-baf3c3f41f7a5861c8ab33c0a8a9e4c73d5241cc9af56ccf7633586f03380a103</cites><orcidid>0000-0002-0018-6170 ; 0000-0002-4193-7612 ; 0000-0002-4255-5472 ; 0000-0003-3940-9439 ; 0000-0001-9379-3027 ; 0000-0002-6244-602X ; 0000-0002-9981-3321</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7216235/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7216235/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27922,27923,53789,53791</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32325956$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zimbone, Stefania</creatorcontrib><creatorcontrib>Santoro, Anna M</creatorcontrib><creatorcontrib>La Mendola, Diego</creatorcontrib><creatorcontrib>Giacomelli, Chiara</creatorcontrib><creatorcontrib>Trincavelli, Maria L</creatorcontrib><creatorcontrib>Tomasello, Marianna F</creatorcontrib><creatorcontrib>Milardi, Danilo</creatorcontrib><creatorcontrib>García-Viñuales, Sara</creatorcontrib><creatorcontrib>Sciacca, Michele F M</creatorcontrib><creatorcontrib>Martini, Claudia</creatorcontrib><creatorcontrib>Grasso, Giulia</creatorcontrib><title>The Ionophoric Activity of a Pro-Apoptotic VEGF165 Fragment on HUVEC Cells</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Copper plays an important role as a regulator in many pathologies involving the angiogenesis process. In cancerogenesis, tumor progression, and angiogenic diseases, copper homeostasis is altered. Although many details in the pathways involved are still unknown, some copper-specific ligands have been successfully used as therapeutic agents. Copper-binding peptides able to modulate angiogenesis represent a possible way to value new drugs. We previously reported that a fragment (VEGF73-101) of vascular endothelial growth factor (VEGF165), a potent angiogenic, induced an apoptotic effect on human umbilical vein endothelial cells. The aim of this study was to investigate the putative copper ionophoric activity of VEGF73-101, as well as establish a relationship between the structure of the peptide fragment and the cytotoxic activity in the presence of copper(II) ions. Here, we studied the stoichiometry and the conformation of the VEGF73-101/Cu(II) complexes and some of its mutated peptides by electrospray ionization mass spectrometry and circular dichroism spectroscopy. Furthermore, we evaluated the effect of all peptides in the absence and presence of copper ions by cell viability and cytofuorimetric assays. The obtained results suggest that VEGF73-101 could be considered an interesting candidate in the development of new molecules with ionophoric properties as agents in antiangiogenic therapeutic approaches.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Angiogenesis</subject><subject>Antiangiogenics</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis - genetics</subject><subject>Cell Membrane Permeability</subject><subject>Cell Survival - drug effects</subject><subject>Cell viability</subject><subject>Chelating Agents - pharmacology</subject><subject>Chemical compounds</subject><subject>Chromatography</subject><subject>Circular dichroism</subject><subject>Conformation</subject><subject>Copper - metabolism</subject><subject>Copper compounds</subject><subject>Cytotoxicity</subject><subject>Dichroism</subject><subject>Endothelial cells</subject><subject>Growth factors</subject><subject>Homeostasis</subject><subject>Human Umbilical Vein Endothelial Cells - 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In cancerogenesis, tumor progression, and angiogenic diseases, copper homeostasis is altered. Although many details in the pathways involved are still unknown, some copper-specific ligands have been successfully used as therapeutic agents. Copper-binding peptides able to modulate angiogenesis represent a possible way to value new drugs. We previously reported that a fragment (VEGF73-101) of vascular endothelial growth factor (VEGF165), a potent angiogenic, induced an apoptotic effect on human umbilical vein endothelial cells. The aim of this study was to investigate the putative copper ionophoric activity of VEGF73-101, as well as establish a relationship between the structure of the peptide fragment and the cytotoxic activity in the presence of copper(II) ions. Here, we studied the stoichiometry and the conformation of the VEGF73-101/Cu(II) complexes and some of its mutated peptides by electrospray ionization mass spectrometry and circular dichroism spectroscopy. Furthermore, we evaluated the effect of all peptides in the absence and presence of copper ions by cell viability and cytofuorimetric assays. The obtained results suggest that VEGF73-101 could be considered an interesting candidate in the development of new molecules with ionophoric properties as agents in antiangiogenic therapeutic approaches.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>32325956</pmid><doi>10.3390/ijms21082866</doi><orcidid>https://orcid.org/0000-0002-0018-6170</orcidid><orcidid>https://orcid.org/0000-0002-4193-7612</orcidid><orcidid>https://orcid.org/0000-0002-4255-5472</orcidid><orcidid>https://orcid.org/0000-0003-3940-9439</orcidid><orcidid>https://orcid.org/0000-0001-9379-3027</orcidid><orcidid>https://orcid.org/0000-0002-6244-602X</orcidid><orcidid>https://orcid.org/0000-0002-9981-3321</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Angiogenesis Antiangiogenics Apoptosis Apoptosis - drug effects Apoptosis - genetics Cell Membrane Permeability Cell Survival - drug effects Cell viability Chelating Agents - pharmacology Chemical compounds Chromatography Circular dichroism Conformation Copper - metabolism Copper compounds Cytotoxicity Dichroism Endothelial cells Growth factors Homeostasis Human Umbilical Vein Endothelial Cells - metabolism Humans Hydrophobic and Hydrophilic Interactions Kinases Ligands Mass spectrometry Mass spectroscopy Mutation Neovascularization, Physiologic - drug effects Neovascularization, Physiologic - genetics Peptide Fragments - chemistry Peptide Fragments - pharmacology Peptides Permeability Pharmacology Protein Binding Protein Conformation Retention Spectrometry, Mass, Electrospray Ionization Spectrum Analysis Stoichiometry Structure-Activity Relationship Umbilical vein Vascular endothelial growth factor Vascular Endothelial Growth Factor A - chemistry Vascular Endothelial Growth Factor A - genetics Vascular Endothelial Growth Factor A - metabolism Vascular Endothelial Growth Factor A - pharmacology |
| title | The Ionophoric Activity of a Pro-Apoptotic VEGF165 Fragment on HUVEC Cells |
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