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Complexation of Lysozyme with Poly(sodium(sulfamate-carboxylate)isoprene)

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Complexation of Lysozyme with Poly(sodium(sulfamate-carboxylate)isoprene)
Πίσπας, Στέργιος
Nounesis, George
Karayianni, Maria
Γκιώνης, Βασίλης
Χρυσικός, Γεώργιος Δ.
Giatrellis, Sarantis
Άρθρο σε επιστημονικό περιοδικό
2011-05
The complexation between hen egg white lysozyme (HEWL) and a novel pH-sensitive and intrinsically hydrophobic polyelectrolyte poly(sodium(sulfamate-carboxylate)isoprene) (SCPI), was investigated by means of dynamic, static, and electrophoretic light scattering and isothermal titration calorimetry measurements. The complexation process was studied at both pH 7 and 3 (high and low charge density of the SCPI, respectively) and under low ionic strength conditions for two polyelectrolyte samples of different molecular weights. The solution behavior, structure, and effective charge of the formed complexes proved to be dependent on the pH, the [-]/[+] charge ratio, and the molecular weight of the polyelectrolyte. Increasing the ionic strength of the solution led to vast aggregation and eventually precipitation of the complexes. The interaction between HEWL and SCPI was found to be mainly electrostatic, associated with an exothermic enthalpy change. The structural investigation of the complexed protein by fluorescence, infrared, circular dichroism spectroscopic, and differential scanning calorimetric measurements revealed no signs of denaturation upon complexation.
Washington
Οργανική χημεία (EL)
Βιολογία (Γενικά) (EL)
Χημεία (Γενικά) (EL)
Biology (General) (EN)
Organic chemistry (EN)
Chemistry (General) (EN)
Polymer Science
English
American Chemical Society
Biomacromolecules
© AMER CHEMICAL SOC
© AMER CHEMICAL SOC (EN)
National Hellenic Research Foundation (NHRF)
Helios - Repository of the National Hellenic Research Foundation (NHRF)



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