Protein-polymer conjugates are a blooming class of hybrid systems with high biomedical potential. Despite a plethora of papers on their biomedical properties, the physical–chemical characterization of many protein-polymer conjugates is missing. Here, we evaluated the thermal stability of a set of fully-degradable polyphosphoester-protein conjugates by variable temperature circular dichroism, a common but powerful technique. We extensively describe their thermodynamic stability in different environments (in physiological buffer or in presence of chemical denaturants, e.g., acid or urea), highlighting the protective role of the polymer in preserving the protein from denaturation. For the first time, we propose a simple but effective protocol to achieve useful information on these systems in vitro, useful to screen new samples in their early stages.

A circular dichroism study of the protective role of polyphosphoesters polymer chains in polyphosphoester‐myoglobin conjugates

Pelosi, Chiara
Primo
;
Arrico, Lorenzo;Zinna, Francesco
;
Di Bari, Lorenzo;Tinè, Maria R.
2022-01-01

Abstract

Protein-polymer conjugates are a blooming class of hybrid systems with high biomedical potential. Despite a plethora of papers on their biomedical properties, the physical–chemical characterization of many protein-polymer conjugates is missing. Here, we evaluated the thermal stability of a set of fully-degradable polyphosphoester-protein conjugates by variable temperature circular dichroism, a common but powerful technique. We extensively describe their thermodynamic stability in different environments (in physiological buffer or in presence of chemical denaturants, e.g., acid or urea), highlighting the protective role of the polymer in preserving the protein from denaturation. For the first time, we propose a simple but effective protocol to achieve useful information on these systems in vitro, useful to screen new samples in their early stages.
2022
Pelosi, Chiara; Arrico, Lorenzo; Zinna, Francesco; Wurm, Frederik R.; Di Bari, Lorenzo; Tinè, Maria R.
File in questo prodotto:
File Dimensione Formato  
2_Chirality_Pelosi et al..pdf

accesso aperto

Descrizione: Final manuscript
Tipologia: Versione finale editoriale
Licenza: Creative commons
Dimensione 2.97 MB
Formato Adobe PDF
2.97 MB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11568/1146861
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 1
  • ???jsp.display-item.citation.isi??? 0
social impact