Short PlGF-derived peptides bind VEGFR-1 and VEGFR-2 in vitro and on the surface of endothelial cells (361 views)
J Pept Sci (ISSN: 1075-2617linking, 1099-1387electronic), 2019 May; 25 (5 ): e3146-e3146.
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Paper type: Journal Article,
Impact factor: 1.807, 5-year impact factor: 1.872
Url: Not available.
Keywords: Cd , Plgf Peptides , Spr , Vegf Receptors , Cell-Based Assays,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR and CIRPEB, Naples, Italy.
SensiQ Technologies, Inc., 800 Research Pkwy, Oklahoma City, OK, 73104, USA.
Dipartimento di Farmacia, Universita degli Studi di Napoli "Federico II", Naples, Italy.
References:
Not available.
J Pept Sci (ISSN: 1075-2617linking, 1099-1387electronic), 2019 May; 25 (5 ): e3146-e3146.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.807, 5-year impact factor: 1.872
Url: Not available.
Keywords: Cd , Plgf Peptides , Spr , Vegf Receptors , Cell-Based Assays,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR and CIRPEB, Naples, Italy.
SensiQ Technologies, Inc., 800 Research Pkwy, Oklahoma City, OK, 73104, USA.
Dipartimento di Farmacia, Universita degli Studi di Napoli "Federico II", Naples, Italy.
References:
Not available.
Short PlGF-derived peptides bind VEGFR-1 and VEGFR-2 in vitro and on the surface of endothelial cells
The placental growth factor (PlGF), a member of VEGF family, plays a crucial role in pathological angiogenesis, especially ischemia, inflammation, and cancer. This activity is mediated by its selective binding to VEGF receptor 1 (VEGFR-1), which occurs predominantly through receptor domains 2 and 3. The PlGF beta-hairpin region spanning residues Q87 to V100 is one of the key binding elements on the protein side. We have undertaken a study on the design, preparation, and functional characterization of the peptide reproducing this region and of a set of analogues where glycine 94, occurring at the corner of the hairpin in the native protein, is replaced by charged as well as hydrophobic residues. Also, some peptides with arginine 96 replaced by other residues have been studied. We find that the parent peptide weakly binds VEGFR-1, but replacement of G94 with residues bearing H-bond donating residues significantly improves the affinity. Replacement of R96 instead blocks the interaction between the peptide and the domain. The strongest affinity is observed with the G94H (peptide PlGF-2) and G94W (peptide PlGF-10) mutants, while the peptide PlGF-8, bearing the R96G mutation, is totally inactive. The PlGF-1 and PlGF-2 peptides also bind the VEGFR-2 receptors, though with a reduced affinity, and are able to interfere with the VEGF-induced receptor signaling on endothelial cells. The peptides also bind VEGFR-2 on the surface of cells, while PlGF-8 is inactive. Data suggest that these peptides have potential applications as PlGF/VEGF mimic in various experimental settings.
The placental growth factor (PlGF), a member of VEGF family, plays a crucial role in pathological angiogenesis, especially ischemia, inflammation, and cancer. This activity is mediated by its selective binding to VEGF receptor 1 (VEGFR-1), which occurs predominantly through receptor domains 2 and 3. The PlGF beta-hairpin region spanning residues Q87 to V100 is one of the key binding elements on the protein side. We have undertaken a study on the design, preparation, and functional characterization of the peptide reproducing this region and of a set of analogues where glycine 94, occurring at the corner of the hairpin in the native protein, is replaced by charged as well as hydrophobic residues. Also, some peptides with arginine 96 replaced by other residues have been studied. We find that the parent peptide weakly binds VEGFR-1, but replacement of G94 with residues bearing H-bond donating residues significantly improves the affinity. Replacement of R96 instead blocks the interaction between the peptide and the domain. The strongest affinity is observed with the G94H (peptide PlGF-2) and G94W (peptide PlGF-10) mutants, while the peptide PlGF-8, bearing the R96G mutation, is totally inactive. The PlGF-1 and PlGF-2 peptides also bind the VEGFR-2 receptors, though with a reduced affinity, and are able to interfere with the VEGF-induced receptor signaling on endothelial cells. The peptides also bind VEGFR-2 on the surface of cells, while PlGF-8 is inactive. Data suggest that these peptides have potential applications as PlGF/VEGF mimic in various experimental settings.
Short PlGF-derived peptides bind VEGFR-1 and VEGFR-2 in vitro and on the surface of endothelial cells
Short PlGF-derived peptides bind VEGFR-1 and VEGFR-2 in vitro and on the surface of endothelial cells
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Calvanese L, Caporale A, Focà G, Iaccarino E, Sandomenico A, Doti N, Apicella I, Incisivo GM, De Falco S, Falcigno L, D’auria G, Ruvo M
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Impact Factor: 2.906
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Diana D, Russomanno A, De Rosa L, Di Stasi R, Capasso D, Di Gaetano S, Romanelli A, Russo L, D'Andrea LD, Fattorusso R
* Functional Binding Surface Of A Beta-Hairpin Vegf Receptor Targeting Peptide Determined By Nmr Spectroscopy In Living Cells (520 views)
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Impact Factor: 5.771
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D’Andrea LD, Fattorusso R, Carannante C, Pedone C
* Targeting VEGF Receptors Using Designed Polypeptide (281 views)
Peptides 2002, 2002; ConferenceBook: 454-455.
Impact Factor: 0
View Export to BibTeX Export to EndNote
* Targeting VEGF receptors with non-neutralizing cyclopeptides for imaging applications (680 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2017 Dec 2; 50(2): 321-329.
Impact Factor: 2.906
View Export to BibTeX Export to EndNote
Diana D, Russomanno A, De Rosa L, Di Stasi R, Capasso D, Di Gaetano S, Romanelli A, Russo L, D'Andrea LD, Fattorusso R
* Functional Binding Surface Of A Beta-Hairpin Vegf Receptor Targeting Peptide Determined By Nmr Spectroscopy In Living Cells (520 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2015 Jan 2; 21(1): 91-95.
Impact Factor: 5.771
View Export to BibTeX Export to EndNote
D’Andrea LD, Fattorusso R, Carannante C, Pedone C
* Targeting VEGF Receptors Using Designed Polypeptide (281 views)
Peptides 2002, 2002; ConferenceBook: 454-455.
Impact Factor: 0
View Export to BibTeX Export to EndNote
3 Records (2 excluding Abstracts).
Total impact factor: 8.677 (8.677 excluding Abstracts).
Total 5 year impact factor: 8.518 (8.518 excluding Abstracts).
Total impact factor: 8.677 (8.677 excluding Abstracts).
Total 5 year impact factor: 8.518 (8.518 excluding Abstracts).
361 views. Last view on Saturday 14 September 2024, 6:30:57
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