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Tesi etd-05182017-171847


Thesis type
Tesi di laurea magistrale
Author
PELOSI, CHIARA
URN
etd-05182017-171847
Title
New developments in protein-polymer conjugation: PPE-ylated myoglobin
Struttura
CHIMICA E CHIMICA INDUSTRIALE
Corso di studi
CHIMICA
Supervisors
relatore Prof.ssa Tinè, Maria Rosaria
relatore Dott. Wurm, Frederik R.
controrelatore Dott.ssa Petri, Antonella
Parole chiave
  • myoglobin
  • n-DSC
  • polyphosphoesyers
  • protein-polymer conjugates
Data inizio appello
15/06/2017;
Consultabilità
Parziale
Data di rilascio
15/06/2020
Riassunto analitico
Protein-polymer conjugates are used to treat several diseases, therefore the design of novel efficient conjugates is very promising for academia and industry. Here, we present the synthesis and characterization of novel PEEP-myoglobin conjugates. PEEP (poly(ethyl ethylene phosphate)) belongs to polyphosphoesters, a class of biocompatible and biodegradable polymers, promising candidate to substitute the “gold standard” poly(ethylene glycol) (PEG) in biomedical field, which can cause long term effects as it is not degradable. PEEP-ylated conjugates with variable polymer chains were synthesized and compared with PEGylated myoglobin, in order to understand how structure, number, length of the polymer influence protein’s features and properties. Measures of activity, absorbance, calorimetry and fluorimetry on the conjugates show a decrease in unfolding temperature and activity, but in all the cases the loss does not affect irremediably the protein’s features under physiological conditions. Furthermore PEG shows to stabilize myoglobin preventing aggregation and increasing the unfolding reversibility. We detected a decreasing trend in observed properties linked to the increase number of chains and polymer length.
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