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

Chiara Pelosi*, Lorenzo Arrico, Francesco Zinna*, Frederik R. Wurm, Lorenzo Di Bari, Maria R. Tinè

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

2 Citations (Scopus)
46 Downloads (Pure)

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.

Original languageEnglish
Pages (from-to)1257-1265
Number of pages9
JournalChirality
Volume34
Issue number9
Early online date17 Jun 2022
DOIs
Publication statusPublished - Sept 2022

Keywords

  • circular dichroism
  • polyphosphoesters
  • protein thermal stability
  • protein unfolding
  • protein-polymer conjugates

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