Antiangiogenic activity and plasma stability study of peptidomimetics containing unnatural proline analogs

Abstract

Biologically active peptides are often considered as leading compounds in the drugs development process. However, the peptide bond is susceptible to enzymatic hydrolysis, thus the peptides may not be entirely stable in body fluids. One of the way to reduce this effect is to design new analogs with modified structure and properties. In general, such compounds are similar to the parent peptide sequence (to preserve biological activity), but structural changes ensure higher degradation resistance due to the enzyme failure of recognizing cleavage site.