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Article

Tween® Preserves Enzyme Activity and Stability in PLGA Nanoparticles

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Te.Far.T.I.-Nanotech Lab, Department of Life Sciences, University of Modena and Reggio Emilia, 41125 Modena, Italy
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Clinical and Experimental Medicine PhD Program, Department of Biomedical, Metabolic and Neural Sciences, University of Modena and Reggio Emilia, 41125 Modena, Italy
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Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna, 40127 Bologna, Italy
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Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544, USA
*
Author to whom correspondence should be addressed.
Academic Editor: José das Neves
Nanomaterials 2021, 11(11), 2946; https://doi.org/10.3390/nano11112946
Received: 31 August 2021 / Revised: 25 October 2021 / Accepted: 28 October 2021 / Published: 3 November 2021
Enzymes, as natural and potentially long-term treatment options, have become one of the most sought-after pharmaceutical molecules to be delivered with nanoparticles (NPs); however, their instability during formulation often leads to underwhelming results. Various molecules, including the Tween® polysorbate series, have demonstrated enzyme activity protection but are often used uncontrolled without optimization. Here, poly(lactic-co-glycolic) acid (PLGA) NPs loaded with β-glucosidase (β-Glu) solutions containing Tween® 20, 60, or 80 were compared. Mixing the enzyme with Tween® pre-formulation had no effect on particle size or physical characteristics, but increased the amount of enzyme loaded. More importantly, NPs made with Tween® 20:enzyme solutions maintained significantly higher enzyme activity. Therefore, Tween® 20:enzyme solutions ranging from 60:1 to 2419:1 mol:mol were further analyzed. Isothermal titration calorimetry analysis demonstrated low affinity and unquantifiable binding between Tween® 20 and β-Glu. Incorporating these solutions in NPs showed no effect on size, zeta potential, or morphology. The amount of enzyme and Tween® 20 in the NPs was constant for all samples, but a trend towards higher activity with higher molar rapports of Tween® 20:β-Glu was observed. Finally, a burst release from NPs in the first hour with Tween®:β-Glu solutions was the same as free enzyme, but the enzyme remained active longer in solution. These results highlight the importance of stabilizers during NP formulation and how optimizing their use to stabilize an enzyme can help researchers design more efficient and effective enzyme loaded NPs. View Full-Text
Keywords: polymeric nanoparticles; enzyme delivery; enzyme stabilization; Tween® stabilization; nanomedicine polymeric nanoparticles; enzyme delivery; enzyme stabilization; Tween® stabilization; nanomedicine
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MDPI and ACS Style

Duskey, J.T.; Ottonelli, I.; Rinaldi, A.; Parmeggiani, I.; Zambelli, B.; Wang, L.Z.; Prud’homme, R.K.; Vandelli, M.A.; Tosi, G.; Ruozi, B. Tween® Preserves Enzyme Activity and Stability in PLGA Nanoparticles. Nanomaterials 2021, 11, 2946. https://doi.org/10.3390/nano11112946

AMA Style

Duskey JT, Ottonelli I, Rinaldi A, Parmeggiani I, Zambelli B, Wang LZ, Prud’homme RK, Vandelli MA, Tosi G, Ruozi B. Tween® Preserves Enzyme Activity and Stability in PLGA Nanoparticles. Nanomaterials. 2021; 11(11):2946. https://doi.org/10.3390/nano11112946

Chicago/Turabian Style

Duskey, Jason Thomas, Ilaria Ottonelli, Arianna Rinaldi, Irene Parmeggiani, Barbara Zambelli, Leon Z. Wang, Robert K. Prud’homme, Maria Angela Vandelli, Giovanni Tosi, and Barbara Ruozi. 2021. "Tween® Preserves Enzyme Activity and Stability in PLGA Nanoparticles" Nanomaterials 11, no. 11: 2946. https://doi.org/10.3390/nano11112946

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