Authors Ciolkowski, M. ; Palecz, B. ; Appelhans, D. ; Voit, B. ; Klajnert, B. ; Bryszewska, M.
Title The influence of maltose modified poly(propylene imine) dendrimers on hen egg white lysozyme structure and thermal stability
Date 09.05.2012
Number 32742
Abstract In this study the influence of dendrimers’ surface modification upon the strength of interaction with proteins was examined. Unmodified, cationic poly(propylene imine) dendrimer of the fourth generation (PPI G4), two PPI G4 dendrimers, partially and fully coated with maltose residues, and anionic polyamidoamine dendrimer of the third and a half generation (PAMAM G3.5 dendrimer), were used in the study. Hen egg white lysozyme, which possesses a cationic net charge under physiological conditions, was chosen as a model protein. The influence of dendrimers on the thermal stability of lysozyme was studied using differential scanning calorimetry (DSC) and circular dichroism (CD) methods. Additionally, the effect of dendrimers on the availability of lysozyme tryptophan residues to fluorescence quenchers was examined. It was shown that modification of dendrimer surface with maltose reduced its influence on lysozyme properties. However, even full surface modification, resulting in a neutral surface charge, did not deprive dendrimer of the ability to interact with the protein. It was probably caused by the introduction of a large number of hydroxyl groups from maltose residues on the surface of the dendrimer. In the study a comparable strength of influence exerted on lysozyme by cationic PPI dendrimer and anionic PAMAM G3.5 dendrimer was observed. The possible explanation of this fact is the presence of both positively and negatively charged areas on the surface of lysozyme. Such areas allow dendrimers possessing opposite surface charges to interact with lysozyme.
Publisher Colloids and Surfaces B: Biointerfaces
Citation Colloids and Surfaces B: Biointerfaces 95 (2012) 103-108
Tags ppi dendrimers maltose modified dendrimers lysozyme dendrimer–protein interaction fluorescence quenching bovine serum-albumin circular-dichroism secondary structure pamam dendrimers proteins binding

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