The remarkable stability of chimeric, sialic acid-derived alpha/delta-peptides in human blood plasma.

ABSTRACT: Peptides are labile toward proteolytic enzymes, and structural modifications are often required to prolong their metabolic half-life and increase resistance. One modification is the incorporation of non-alpha-amino acids into the peptide to deter recognition by hydrolytic enzymes. We previously reported the synthesis of chimeric alpha/delta-peptides from glutamic acids (Glu) and the sialic acid derivative Neu2en. Conformational analyses revealed these constructs adopt secondary structures in water and may serve as conformational surrogates of polysialic acid. Polysialic acid is a tumor-associated polysaccharide and is correlated with cancer metastasis. Soluble polysialic acid is rapidly cleared from the blood limiting its potential for vaccine development. One motivation in developing stru

SUBMITTER: Saludes JP 

PROVIDER: S-EPMC4504198 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature