Mucosomes: Intrinsically Mucoadhesive Glycosylated Mucin Nanoparticles as Multi‐Drug Delivery Platform
Abstract: Mucus is a complex barrier for pharmacological treatments and overcoming it is one of the major challenges faced during transmucosal drug delivery. To tackle this issue, a novel class of glycosylated nanoparticles, named “mucosomes,” which are based on the most important protein constituting mucus, the mucin, is introduced. Mucosomes are designed to improve drug absorption and residence time on the mucosal tissues. Mucosomes are produced (150–300 nm), functionalized with glycans, and loaded with the desired drug in a single one‐pot synthetic process and, with this method, a wide range of small and macro molecules can be loaded with different physicochemical properties. Various in vitro models are used to test the mucoadhesive properties of mucosomes. The presence of functional glycans is indicated by the interaction with lectins. Mucosomes are proven to be storable at 4 °C after lyophilization, and administration through a nasal spray does not modify the morphology of the mucosomes. In vitro and in vivo tests indicate mucosomes do not induce adverse effects under the investigated conditions. This study proposes mucosomes as a ground‐breaking nanosystem that can be applied in several pathological contexts, especially in mucus‐related disorders.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Mucosomes: Intrinsically Mucoadhesive Glycosylated Mucin Nanoparticles as Multi‐Drug Delivery Platform ; day:04 ; month:06 ; year:2022 ; extent:18
Advanced healthcare materials ; (04.06.2022) (gesamt 18)
- Creator
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Butnarasu, Cosmin
Petrini, Paola
Bracotti, Francesco
Visai, Livia
Guagliano, Giuseppe
Fiorio Pla, Alessandra
Sansone, Ettore
Petrillo, Sara
Visentin, Sonja
- DOI
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10.1002/adhm.202200340
- URN
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urn:nbn:de:101:1-2022060415412875228623
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:28 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Butnarasu, Cosmin
- Petrini, Paola
- Bracotti, Francesco
- Visai, Livia
- Guagliano, Giuseppe
- Fiorio Pla, Alessandra
- Sansone, Ettore
- Petrillo, Sara
- Visentin, Sonja
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Synthesis of glycosylated β3-homo-threonine conjugates for mucin-like glycopeptide antigen analogues
Effect of O-glycans on the Structure and Viscosity of Intrinsically Disordered and Glycosylated Protein Lubricin
NmeCas9 is an intrinsically high-fidelity genome-editing platform
Engineering of N. benthamianaL. plants for production of N-acetylgalactosamine-glycosylated proteins - towards development of a plant-based platform for production of protein therapeutics with mucin type O-glycosylation
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Mass spectrometric sequencing of O-glycosylated peptides
Synthesis of N‐Glycosylated Soluble Fas Ligand
Exposing the molecular heterogeneity of glycosylated biotherapeutics
Development of differentially glycosylated IgG antibodies
Liver and muscle hemojuvelin are differently glycosylated
Relationship Between Estimated Glycosylated Hemoglobin Using Flash Glucose Monitoring and Actual Measured Glycosylated Hemoglobin in a Chinese Population
TFEB intrinsically regulates mitochondrial functions
Synthesis of glycosylated β3-homo-threonine conjugates for mucin-like glycopeptide antigen analogues
Effect of O-glycans on the Structure and Viscosity of Intrinsically Disordered and Glycosylated Protein Lubricin
NmeCas9 is an intrinsically high-fidelity genome-editing platform
Engineering of N. benthamianaL. plants for production of N-acetylgalactosamine-glycosylated proteins - towards development of a plant-based platform for production of protein therapeutics with mucin type O-glycosylation
Intrinsically bad gratitude
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