Peptide Folding
The process by which a linear chain of amino acids adopts its functional three-dimensional conformation. Correct folding is essential for biological activity — misfolded peptides may be inactive, unstable, or potentially immunogenic. Manufacturing processes must ensure proper folding of therapeutic peptides.
Technical Context
Correct folding is driven by the amino acid sequence (Anfinsen's dogma — the sequence contains all information needed for folding) and influenced by environmental conditions (pH, temperature, ionic strength, redox state). Misfolded peptides may be biologically inactive, prone to aggregation, or immunogenic. In recombinant production, misfolding can lead to inclusion body formation in bacterial hosts, requiring denaturation and refolding steps. For synthetic peptides with disulphide bonds, oxidative folding must produce the correct disulphide bond pattern among multiple possible arrangements. Quality control methods including circular dichroism and NMR spectroscopy can assess peptide folding.