β-amino acid substitution in the SIINFEKL antigen alters immunological recognition.

ABSTRACT:

Background

Peptide vaccines offer a direct way to initiate an immunogenic response to a defined antigen epitope. However, peptide vaccines are unstable in vivo, subject to rapid enzymatic proteolysis. Replacement of an α-amino acid residue with a homologous β-amino acid residue (native side chain, but backbone extended by a single CH₂ unit) impairs proteolysis at nearby amide bonds. Therefore, antigen analogues containing α-to-β replacements have been examined for functional mimicry of native all-α antigens. Another group previously took this approach in the ovalbumin (OVA) antigen model by evaluating single α-to-β analogues of the murine major histocompatibility complex (MHC) I-restricted peptide SIINFEKL.

Methods

We re-examined this set of α/β SIINFEKL an

SUBMITTER: Rastogi I 

PROVIDER: S-EPMC11988276 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature