Enhanced Diagnostic Tools
Chemically synthetised peptides carry free amino and carboxy termini, being electrically charged in general. In order to remove this electric charge, peptide ends are often modified by N-terminal acetylation and/or C-terminal amidation.
peptide ends are uncharged, compared to standard synthetic peptides, so they mimic natural peptides; permeability of cells increases
stability toward digestions by aminopeptidases is enhanced
peptide ends are blocked against synthetase activities
acetylated peptides serve as optimized enzyme substrates
amidation of peptides enhances activity of peptide hormones
intracellular, in-vivo assays (e.g., microbiology)
in-vivo or in-vitro functional studies (activity of peptides or peptidic molecules)
ELISA assays – in order to minimize influences of charged C- or N-termini with ELISA binding characteristics
Both N-terminal acetylation and C-terminal amidation block the respective terminus for coupling of additional modifications, such as dyes, functional groups, etc. However, when requiring additional terminal modifications, the only possibility is to couple these modifications via a functional group within the side-chain of the N- or Cterminal amino acids.
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