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Sodium alginate (SA), acting as a trypsin inhibitor by means of electrostatic interaction, is studied. The half-maximal inhibitory concentration (IC50 = 0.05 μg mL(-1) ) of this natural anionic polymer is about 400 times lower than that of commercial soybean trypsin inhibitor (STI). Unlike the Ca(2+) -deprivation mechanisms, its inhibition may be attributed to preventing the trypsin active site (TAS) from accessing the macromolecular substrates instead of denaturing it. SA is an efficient, innocuous, and cost-effective inhibitory excipient that can be conveniently used in many peptide and protein dosage formulations., (© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

We report on an iconoclastic strategy for inhibiting proteases via autolysis acceleration. We show that proteases can be concentrated and induced to rapidly self-digest by a biocompatible polymer serving as an efficient catalyst. This new generation of protease inhibitors may find applications in the treatment of various protease-dependent diseases. [ABSTRACT FROM AUTHOR]

Front Cover: A natural anionic polymer sodium alginate is applied to protect insulin from trypsin degradation in the human small intestine. Such an inhibitor can be used in all kinds of dosage forms. Its mechanism may be attributed to preventing tryptic active sites from accessing the macromolecular substrates. Further details can be found in the article by Y. Lv, J. B. Zhang, Y. Z. Song, B. Wang, S. J. Wang, S. Zhao, G. J. Lv,* and X. J. Ma* on page 1606. [ABSTRACT FROM AUTHOR]