Mechanistic Insight into the Binding and Swelling Functions of Prepeptidase C-Terminal (PPC) Domains from Various Bacterial Proteases.

The bacterial prepeptidase C-terminal (PPC) domain can be found in the C termini of a wide variety of proteases that are secreted by marine bacteria. However, the functions of these PPC domains remain unknown due to a lack of systematic research. Here, the binding and swelling abilities of eight PPC domains from six different proteases were compared systematically via scanning electron microscopy (SEM), enzyme assays, and fluorescence spectroscopy.

New method of detecting hydrophobic interaction between C-terminal binding domain and biomacromolecules.

The C-terminal domains of proteases play crucial roles in hydrolysis, substrate adsorption and targeted binding. Identifying and characterizing interactions between C-terminal domains and biomacromolecules can help to examine the diversity as well as the substrate-binding ability of C-terminal domains and to explore novel functions. The bacterial pre-peptidase C-terminal (PPC) domain is a typical C-terminal domain normally found at the C-terminus of bacterial secreted proteases.

Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins.

Hypertension is now a major problem threatening people health in the world. Angiotensin-I-converting enzyme (ACE) plays an important physiological role in regulation of blood pressure via conversion of angiotensin I to angiotensin II. Inhibition of ACE may have an antihypertensive effect as a consequence of a decrease in blood pressure.