The influence of PAMAM dendrimers surface groups on their interaction with porcine pepsin |
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Authors: | Michal Ciolkowski Monika Rozanek Maria BryszewskaBarbara Klajnert |
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Affiliation: | Department of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, 141/143 Pomorska St., 90-236 Lodz, Poland |
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Abstract: | In this study the ability of three polyamidoamine (PAMAM) dendrimers with different surface charge (positive, neutral and negative) to interact with a negatively charged protein (porcine pepsin) was examined. It was shown that the dendrimer with a positively charged surface (G4 PAMAM-NH2), as well as the dendrimer with a neutral surface (G4 PAMAM-OH), were able to inhibit enzymatic activity of pepsin. It was also found that these dendrimers act as mixed partially non-competitive pepsin inhibitors. The negatively charged dendrimer (G3.5 PAMAM-COOH) was not able to inhibit the enzymatic activity of pepsin, probably due to the electrostatic repulsion between this dendrimer and the protein. No correlation between changes in enzymatic activity of pepsin and alterations in CD spectrum of the protein was observed. It indicates that the interactions between dendrimers and porcine pepsin are complex, multidirectional and not dependent only on disturbances of the secondary structure. |
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Keywords: | PAMAM, polyamidoamine G4 PAMAM-NH2, fourth generation PAMAM dendrimer with amine terminal groups G4 PAMAM-OH, fourth generation PAMAM dendrimer with hydroxyl terminal groups G3.5 PAMAM-COOH, third and a half generation PAMAM dendrimer with carboxyl terminal groups CD, circular dichroism MRE, mean residue elipticity ATP-ase, adenosine triphosphatase |
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