Differential stability of therapeutic peptides with different proteolytic cleavage sites in blood, plasma and serum.

ABSTRACT: Proteolytic degradation of peptide-based drugs is often considered as major weakness limiting systemic therapeutic applications. Therefore, huge efforts are typically devoted to stabilize sequences against proteases present in serum or plasma, obtained as supernatants after complete blood coagulation or centrifugation of blood supplemented with anticoagulants, respectively. Plasma and serum are reproducibly obtained from animals and humans allowing consistent for clinical analyses and research applications. However, the spectrum of active or activated proteases appears to vary depending on the activation of proteases and cofactors during coagulation (serum) or inhibition of such enzymes by anticoagulants (plasma), such as EDTA (metallo- and Ca2+-dependent proteases) and heparin (e.g. throm

SUBMITTER: Bottger R 

PROVIDER: S-EPMC5456363 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature