CXCL5 Modified Nanoparticle Surface Improves CXCR2 + Cell Selective Internalization
Driving nanomaterials to specific cell populations is still a major challenge for different biomedical applications. Several strategies to improve cell binding and uptake have been tried thus far by intrinsic material modifications or decoration with active molecules onto their surface. In the prese...
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Published in | Cells (Basel, Switzerland) Vol. 9; no. 1; p. 56 |
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Abstract | Driving nanomaterials to specific cell populations is still a major challenge for different biomedical applications. Several strategies to improve cell binding and uptake have been tried thus far by intrinsic material modifications or decoration with active molecules onto their surface. In the present work, we covalently bound the chemokine CXCL5 on fluorescently labeled amino-functionalized SiO
nanoparticles to precisely targeting CXCR2
immune cells. We synthesized and precisely characterized the physicochemical features of the modified particles. The presence of CXCL5 on the surface was detected by z-potential variation and CXCL5-specific electron microscopy immunogold labeling. CXCL5-amino SiO
nanoparticle cell binding and internalization performances were analyzed in CXCR2
THP-1 cells by flow cytometry and confocal microscopy. We showed improved internalization of the chemokine modified particles in the absence or the presence of serum. This internalization was reduced by cell pre-treatment with free CXCL5. Furthermore, we demonstrated CXCR2
cell preferential targeting by comparing particle uptake in THP-1 vs. low-CXCR2 expressing HeLa cells. Our results provide the proof of principle that chemokine decorated nanomaterials enhance uptake and allow precise cell subset localization. The possibility to aim at selective chemokine receptor-expressing cells can be beneficial for the diverse pathological conditions involving immune reactions. |
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AbstractList | Driving nanomaterials to specific cell populations is still a major challenge for different biomedical applications. Several strategies to improve cell binding and uptake have been tried thus far by intrinsic material modifications or decoration with active molecules onto their surface. In the present work, we covalently bound the chemokine CXCL5 on fluorescently labeled amino-functionalized SiO
nanoparticles to precisely targeting CXCR2
immune cells. We synthesized and precisely characterized the physicochemical features of the modified particles. The presence of CXCL5 on the surface was detected by z-potential variation and CXCL5-specific electron microscopy immunogold labeling. CXCL5-amino SiO
nanoparticle cell binding and internalization performances were analyzed in CXCR2
THP-1 cells by flow cytometry and confocal microscopy. We showed improved internalization of the chemokine modified particles in the absence or the presence of serum. This internalization was reduced by cell pre-treatment with free CXCL5. Furthermore, we demonstrated CXCR2
cell preferential targeting by comparing particle uptake in THP-1 vs. low-CXCR2 expressing HeLa cells. Our results provide the proof of principle that chemokine decorated nanomaterials enhance uptake and allow precise cell subset localization. The possibility to aim at selective chemokine receptor-expressing cells can be beneficial for the diverse pathological conditions involving immune reactions. Driving nanomaterials to specific cell populations is still a major challenge for different biomedical applications. Several strategies to improve cell binding and uptake have been tried thus far by intrinsic material modifications or decoration with active molecules onto their surface. In the present work, we covalently bound the chemokine CXCL5 on fluorescently labeled amino-functionalized SiO 2 nanoparticles to precisely targeting CXCR2 + immune cells. We synthesized and precisely characterized the physicochemical features of the modified particles. The presence of CXCL5 on the surface was detected by z-potential variation and CXCL5-specific electron microscopy immunogold labeling. CXCL5-amino SiO 2 nanoparticle cell binding and internalization performances were analyzed in CXCR2 + THP-1 cells by flow cytometry and confocal microscopy. We showed improved internalization of the chemokine modified particles in the absence or the presence of serum. This internalization was reduced by cell pre-treatment with free CXCL5. Furthermore, we demonstrated CXCR2 + cell preferential targeting by comparing particle uptake in THP-1 vs. low-CXCR2 expressing HeLa cells. Our results provide the proof of principle that chemokine decorated nanomaterials enhance uptake and allow precise cell subset localization. The possibility to aim at selective chemokine receptor-expressing cells can be beneficial for the diverse pathological conditions involving immune reactions. Driving nanomaterials to specific cell populations is still a major challenge for different biomedical applications. Several strategies to improve cell binding and uptake have been tried thus far by intrinsic material modifications or decoration with active molecules onto their surface. In the present work, we covalently bound the chemokine CXCL5 on fluorescently labeled amino-functionalized SiO2 nanoparticles to precisely targeting CXCR2+ immune cells. We synthesized and precisely characterized the physicochemical features of the modified particles. The presence of CXCL5 on the surface was detected by z-potential variation and CXCL5-specific electron microscopy immunogold labeling. CXCL5-amino SiO2 nanoparticle cell binding and internalization performances were analyzed in CXCR2+ THP-1 cells by flow cytometry and confocal microscopy. We showed improved internalization of the chemokine modified particles in the absence or the presence of serum. This internalization was reduced by cell pre-treatment with free CXCL5. Furthermore, we demonstrated CXCR2+ cell preferential targeting by comparing particle uptake in THP-1 vs. low-CXCR2 expressing HeLa cells. Our results provide the proof of principle that chemokine decorated nanomaterials enhance uptake and allow precise cell subset localization. The possibility to aim at selective chemokine receptor-expressing cells can be beneficial for the diverse pathological conditions involving immune reactions. |
Author | Catalano, Federico Bardi, Giuseppe Sanchez-Moreno, Paola Pompa, Pier Paolo Cibecchini, Giulia Gatto, Francesca Marotta, Roberto Cagliani, Roberta |
AuthorAffiliation | 2 Department of Chemistry and Industrial Chemistry, University of Genova, Via Dodecaneso 31, 16146 Genova, Italy 3 Electron Microscopy Laboratory, Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genova, Italy; roberto.marotta@iit.it (R.M.); federico.catalano@iit.it (F.C.) 1 Nanobiointeractions & Nanodiagnostics, Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genova, Italy; roberta.cagliani@iit.it (R.C.); francesca.gatto@iit.it (F.G.); giulia.cibecchini@iit.it (G.C.); paola.sanchez@iit.it (P.S.-M.); pierpaolo.pompa@iit.it (P.P.P.) |
AuthorAffiliation_xml | – name: 1 Nanobiointeractions & Nanodiagnostics, Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genova, Italy; roberta.cagliani@iit.it (R.C.); francesca.gatto@iit.it (F.G.); giulia.cibecchini@iit.it (G.C.); paola.sanchez@iit.it (P.S.-M.); pierpaolo.pompa@iit.it (P.P.P.) – name: 3 Electron Microscopy Laboratory, Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genova, Italy; roberto.marotta@iit.it (R.M.); federico.catalano@iit.it (F.C.) – name: 2 Department of Chemistry and Industrial Chemistry, University of Genova, Via Dodecaneso 31, 16146 Genova, Italy |
Author_xml | – sequence: 1 givenname: Roberta surname: Cagliani fullname: Cagliani, Roberta organization: Department of Chemistry and Industrial Chemistry, University of Genova, Via Dodecaneso 31, 16146 Genova, Italy – sequence: 2 givenname: Francesca surname: Gatto fullname: Gatto, Francesca organization: Nanobiointeractions & Nanodiagnostics, Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genova, Italy – sequence: 3 givenname: Giulia surname: Cibecchini fullname: Cibecchini, Giulia organization: Department of Chemistry and Industrial Chemistry, University of Genova, Via Dodecaneso 31, 16146 Genova, Italy – sequence: 4 givenname: Roberto surname: Marotta fullname: Marotta, Roberto organization: Electron Microscopy Laboratory, Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genova, Italy – sequence: 5 givenname: Federico surname: Catalano fullname: Catalano, Federico organization: Electron Microscopy Laboratory, Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genova, Italy – sequence: 6 givenname: Paola surname: Sanchez-Moreno fullname: Sanchez-Moreno, Paola organization: Nanobiointeractions & Nanodiagnostics, Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genova, Italy – sequence: 7 givenname: Pier Paolo surname: Pompa fullname: Pompa, Pier Paolo organization: Nanobiointeractions & Nanodiagnostics, Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genova, Italy – sequence: 8 givenname: Giuseppe surname: Bardi fullname: Bardi, Giuseppe organization: Nanobiointeractions & Nanodiagnostics, Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genova, Italy |
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CitedBy_id | crossref_primary_10_3390_nano12203560 crossref_primary_10_3389_fbioe_2020_00906 crossref_primary_10_3390_nano10112304 crossref_primary_10_37349_ei_2022_00073 crossref_primary_10_3390_cancers13246293 crossref_primary_10_37349_ei_2021_00006 crossref_primary_10_1002_adfm_202408436 |
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Keywords | immune cells chemokine receptors nanoparticles surface chemistry chemokines |
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StartPage | 56 |
SubjectTerms | Amino acids Cell surface Chemokine receptors Chemokines Confocal microscopy CXCR2 protein Electron microscopy Flow cytometry immune cells Internalization Localization Medical prognosis Microscopy Nanomaterials Nanoparticles Nanotechnology Particle size Penicillin Peptides Physiology Proteins Silicon dioxide surface chemistry |
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Title | CXCL5 Modified Nanoparticle Surface Improves CXCR2 + Cell Selective Internalization |
URI | https://www.ncbi.nlm.nih.gov/pubmed/31878341 https://www.proquest.com/docview/2548364266/abstract/ https://search.proquest.com/docview/2331255401 https://pubmed.ncbi.nlm.nih.gov/PMC7016632 https://doaj.org/article/ab8ec1e3250641f3a88e76e2c66ced01 |
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