Estimating peptide half-life in serum from tunable, sequence-related physicochemical properties.

ABSTRACT: Proteolytic instability is a critical limitation for peptide-based products. Although significant efforts are devoted to stabilize sequences against proteases/peptidases in plasma/serum, such approaches tend to be rather empirical, unspecific, time-consuming, and frequently not cost-effective. A more rational and potentially rewarding alternative is to identify the chemical grounds of susceptibility to enzymatic degradation of peptides so that proteolytic resistance can be tuned by manipulation of key chemical properties. In this regard, we conducted a meta-analysis of literature published over the last decade reporting experimental data on the lifetimes of peptides exposed to proteolytic conditions. Our initial database contained 579 entries and was curated with regard to amino acid seque

SUBMITTER: Cavaco M 

PROVIDER: S-EPMC8301568 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature