A proteome scale study reveals how plastic surfaces and agitation promote protein aggregation
Abstract Protein aggregation in biotherapeutics can reduce their activity and effectiveness. It may also promote immune reactions responsible for severe adverse effects. The impact of plastic materials on protein destabilization is not totally understood. Here, we propose to deconvolve the effects o...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-01-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-023-28412-7 |
| _version_ | 1797945989180424192 |
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| author | Marion Schvartz Florent Saudrais Stéphanie Devineau Jean-Christophe Aude Stéphane Chédin Céline Henry Aarón Millán-Oropeza Thomas Perrault Laura Pieri Serge Pin Yves Boulard Guillaume Brotons Jean-Philippe Renault |
| author_facet | Marion Schvartz Florent Saudrais Stéphanie Devineau Jean-Christophe Aude Stéphane Chédin Céline Henry Aarón Millán-Oropeza Thomas Perrault Laura Pieri Serge Pin Yves Boulard Guillaume Brotons Jean-Philippe Renault |
| author_sort | Marion Schvartz |
| collection | DOAJ |
| description | Abstract Protein aggregation in biotherapeutics can reduce their activity and effectiveness. It may also promote immune reactions responsible for severe adverse effects. The impact of plastic materials on protein destabilization is not totally understood. Here, we propose to deconvolve the effects of material surface, air/liquid interface, and agitation to decipher their respective role in protein destabilization and aggregation. We analyzed the effect of polypropylene, TEFLON, glass and LOBIND surfaces on the stability of purified proteins (bovine serum albumin, hemoglobin and α-synuclein) and on a cell extract composed of 6000 soluble proteins during agitation (P = 0.1–1.2 W/kg). Proteomic analysis revealed that chaperonins, intrinsically disordered proteins and ribosomes were more sensitive to the combined effects of material surfaces and agitation while small metabolic oligomers could be protected in the same conditions. Protein loss observations coupled to Raman microscopy, dynamic light scattering and proteomic allowed us to propose a mechanistic model of protein destabilization by plastics. Our results suggest that protein loss is not primarily due to the nucleation of small aggregates in solution, but to the destabilization of proteins exposed to material surfaces and their subsequent aggregation at the sheared air/liquid interface, an effect that cannot be prevented by using LOBIND tubes. A guidance can be established on how to minimize these adverse effects. Remove one of the components of this combined stress - material, air (even partially), or agitation - and proteins will be preserved. |
| first_indexed | 2024-04-10T21:04:53Z |
| format | Article |
| id | doaj.art-f393109ad0d04f9f9381afbcc098b66e |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-04-10T21:04:53Z |
| publishDate | 2023-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-f393109ad0d04f9f9381afbcc098b66e2023-01-22T12:08:56ZengNature PortfolioScientific Reports2045-23222023-01-0113111710.1038/s41598-023-28412-7A proteome scale study reveals how plastic surfaces and agitation promote protein aggregationMarion Schvartz0Florent Saudrais1Stéphanie Devineau2Jean-Christophe Aude3Stéphane Chédin4Céline Henry5Aarón Millán-Oropeza6Thomas Perrault7Laura Pieri8Serge Pin9Yves Boulard10Guillaume Brotons11Jean-Philippe Renault12Université Paris-Saclay, CEA, CNRS, NIMBE, LIONSUniversité Paris-Saclay, CEA, CNRS, NIMBE, LIONSUniversité Paris Cité, CNRS, Unité de Biologie Fonctionnelle et AdaptativeUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC)Université Paris-Saclay, CEA, CNRS, NIMBE, LIONSUniversité Paris-Saclay, INRAE, AgroParisTech, Micalis Institute, PAPPSOUniversité Paris-Saclay, INRAE, AgroParisTech, Micalis Institute, PAPPSOInstitut des Molécules et Matériaux du Mans (IMMM), UMR 6283 CNRS, Le Mans UniversitéUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC)Université Paris-Saclay, CEA, CNRS, NIMBE, LIONSUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC)Institut des Molécules et Matériaux du Mans (IMMM), UMR 6283 CNRS, Le Mans UniversitéUniversité Paris-Saclay, CEA, CNRS, NIMBE, LIONSAbstract Protein aggregation in biotherapeutics can reduce their activity and effectiveness. It may also promote immune reactions responsible for severe adverse effects. The impact of plastic materials on protein destabilization is not totally understood. Here, we propose to deconvolve the effects of material surface, air/liquid interface, and agitation to decipher their respective role in protein destabilization and aggregation. We analyzed the effect of polypropylene, TEFLON, glass and LOBIND surfaces on the stability of purified proteins (bovine serum albumin, hemoglobin and α-synuclein) and on a cell extract composed of 6000 soluble proteins during agitation (P = 0.1–1.2 W/kg). Proteomic analysis revealed that chaperonins, intrinsically disordered proteins and ribosomes were more sensitive to the combined effects of material surfaces and agitation while small metabolic oligomers could be protected in the same conditions. Protein loss observations coupled to Raman microscopy, dynamic light scattering and proteomic allowed us to propose a mechanistic model of protein destabilization by plastics. Our results suggest that protein loss is not primarily due to the nucleation of small aggregates in solution, but to the destabilization of proteins exposed to material surfaces and their subsequent aggregation at the sheared air/liquid interface, an effect that cannot be prevented by using LOBIND tubes. A guidance can be established on how to minimize these adverse effects. Remove one of the components of this combined stress - material, air (even partially), or agitation - and proteins will be preserved.https://doi.org/10.1038/s41598-023-28412-7 |
| spellingShingle | Marion Schvartz Florent Saudrais Stéphanie Devineau Jean-Christophe Aude Stéphane Chédin Céline Henry Aarón Millán-Oropeza Thomas Perrault Laura Pieri Serge Pin Yves Boulard Guillaume Brotons Jean-Philippe Renault A proteome scale study reveals how plastic surfaces and agitation promote protein aggregation Scientific Reports |
| title | A proteome scale study reveals how plastic surfaces and agitation promote protein aggregation |
| title_full | A proteome scale study reveals how plastic surfaces and agitation promote protein aggregation |
| title_fullStr | A proteome scale study reveals how plastic surfaces and agitation promote protein aggregation |
| title_full_unstemmed | A proteome scale study reveals how plastic surfaces and agitation promote protein aggregation |
| title_short | A proteome scale study reveals how plastic surfaces and agitation promote protein aggregation |
| title_sort | proteome scale study reveals how plastic surfaces and agitation promote protein aggregation |
| url | https://doi.org/10.1038/s41598-023-28412-7 |
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