期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1834, 期 10, 页码 1982-1987出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2013.06.020
关键词
Porcine pepsin; PAMAM dendrimers; Dendrimer-protein interaction; Enzyme inhibition; Circular dichroism
资金
- project Biological properties and biomedical applications of dendrimers [TEAM/2008-1/5]
- EU European Regional Development Fund
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. (C) 2013 Elsevier B.V. All rights reserved.
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