The influence of PAMAM dendrimers surface groups on their interaction with porcine pepsin

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• 作者：Michal Ciolkowski ; Monika Rozanek ; Maria Bryszewska ; Barbara Klajnert
• 关键词：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 ter
• 刊名：Biochimica et Biophysica Acta - Proteins and Proteomics
• 出版年：2013
• 出版时间：October, 2013
• 年：2013
• 卷：1834
• 期：10
• 页码：1982-1987
• 全文大小：699 K

文摘

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.