An effective delivery system is crucial for ensuring the therapeutic efficacy of a drug. This is especially true for biological drugs, which possess unique physicochemical properties and complex pharmacokinetic profiles, and thus require a dedicate design. Whole erythrocytes, and more recently nanoparticles derived from red blood cells (RBCs), have been used in preclinical studies to deliver biological therapeutics: their biocompatibility and extended circulation time help to prevent immunogenicity, and reduce clearance and toxicity. However, characterizing such complex systems poses challenges that complicate their development and optimization. We argue that NMR spectroscopy enables the monitoring of the preservation of the high order structure of the encapsulated proteins, as well as their concentration, thereby assisting in formulation design, development, and manufacturing.
NMR Assessment of the High Order Structure of Biological Therapeutics in Erythrocytes Provides a New Tool for Drug Delivery Design / Luis Padilla Cortés , Giulia Roxana Gheorghita , Francesco Currò, Rebecca Calamandrei, Bianca Susini, Sara Callozzo, Giulia Crivello, Pasquale Russomanno, Enrico Ravera, Linda Cerofolini, Marco Fragai. - ELETTRONICO. - (2025), pp. 1-1. ( "XIVth International conference, NMR: a tool for biology").
NMR Assessment of the High Order Structure of Biological Therapeutics in Erythrocytes Provides a New Tool for Drug Delivery Design
Giulia Roxana Gheorghita;Francesco Currò;Rebecca Calamandrei;Bianca Susini;Sara Callozzo;Pasquale Russomanno;Enrico Ravera;Linda Cerofolini;Marco Fragai
2025
Abstract
An effective delivery system is crucial for ensuring the therapeutic efficacy of a drug. This is especially true for biological drugs, which possess unique physicochemical properties and complex pharmacokinetic profiles, and thus require a dedicate design. Whole erythrocytes, and more recently nanoparticles derived from red blood cells (RBCs), have been used in preclinical studies to deliver biological therapeutics: their biocompatibility and extended circulation time help to prevent immunogenicity, and reduce clearance and toxicity. However, characterizing such complex systems poses challenges that complicate their development and optimization. We argue that NMR spectroscopy enables the monitoring of the preservation of the high order structure of the encapsulated proteins, as well as their concentration, thereby assisting in formulation design, development, and manufacturing.| File | Dimensione | Formato | |
|---|---|---|---|
|
Abstract Parigi.docx
accesso aperto
Tipologia:
Pdf editoriale (Version of record)
Licenza:
Open Access
Dimensione
18.49 kB
Formato
Microsoft Word XML
|
18.49 kB | Microsoft Word XML |
I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.



