LifeTein Free Modifications: N-Terminal Acetylation and C-Terminal Amidation of Peptides

Chemically synthesized peptides carry free amino and carboxy termini. The need for N-terminal acetylation or C-terminal amidation has to be stated explicitly when ordering. It is impossible to perform these modifications after synthesis.

N-terminal acetylation and/or C-terminal amidation reduce the overall charge of a peptide so that the solubility may decrease. But the stability of the peptide could be increased because the terminal acetylation/amidation will generate a closer mimic of the native protein. Thus these modifications may increase the biological activity of a peptide.

Advantages:

• Peptide ends are uncharged so the modifications generate a closer mimic of the native protein thus increasing the permeability of the peptides to cells. This is a good choice of modification for intracellular, in-vivo assay or in-vitro functional studies;
• The modifications increase the metabolic stability of the peptide toward enzymatic degradation by aminopetidases, exopeptidases or synthetase. So the modified peptides can be used as substrates in enzyme assays;
• Amidation of peptides enhances activity of peptide hormones, not only by prolonging their shelf live;
• Reduce influences of charged C or N terminus when ELISA binding assay is conducted.

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