A circular dichroism study of the protective role of polyphosphoesters polymer chains in polyphosphoester‐myoglobin conjugates. Issue 9 (17th June 2022)

• Record Type: Journal Article
• Authors: Pelosi, Chiara; Arrico, Lorenzo; Zinna, Francesco; Wurm, Frederik R.; Di Bari, Lorenzo; Tinè, Maria R.
• Is Part Of: Chirality. Volume 34:Issue 9(2022)
• Page Start: 1257
• Page End: 1265
• Publication Date: 2022-06-17
• Subjects: circular dichroism -- polyphosphoesters -- protein thermal stability -- protein unfolding -- protein‐polymer conjugates; Chirality -- Periodicals; Pharmaceutical chemistry -- Periodicals; 541.22
• DOI: 10.1002/chir.23486
• Languages: English
• ISSNs: 0899-0042

Abstract

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. Abstract : Variable temperature circular dichroism as accessible technique to sceen drug stability Investigation of thermal stability of fully‐degradable protein‐polymer conjugates The protective role of biodegradable polyphosphoesters toward protein in protein‐polymer conjugates