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Abstract
Nanoparticles (NPs) can form a protein corona (PC) with proteins in biological fluids. We examined whether starch nanoparticles (SNPs) form a PC and interact with digestive enzymes in simulated gastric and intestinal fluids. We investigated the adsorption of pepsin and trypsin on unmodified, carboxyl-, and amino-modified SNPs (SNPs, COOH-SNPs, and NH2-SNPs, respectively). Quartz crystal microbalance data showed that a tight and irreversible pepsin corona formed on the NH2-SNPs, pepsin had little or no binding to the SNPs and COOH-SNPs, and trypsin had weak binding to all three kinds of NPs. Dynamic light scattering data showed that pepsin significantly increased the size of the NH2-SNPs from 120 ± 2.6 to 203 ± 12.2 nm and decreased their surface potential from 23.2 ± 1.0 to 12.7 ± 0.2 mV. NH2-SNPs could induce the fluorescence quenching of pepsin and change its secondary structures without affecting its activity.
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