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Peptide design guidelines


Smart Bioscience peptide design guidelines -

The composition in amino acid of a peptide can have various impacts regarding its synthesis or its solubility. Here are few basic things you have to know when designing a peptide:


  • Avoid peptide with more than 50% hydrophobic amino acids content (see section “peptide solubility“). Mutate by polar aa such as Gly or Pro
  • Try to have charged residues in the sequence (R, K, D, E)
  • Basic peptides have to be preferred (positive net charge)
  • Avoid Q (Gln) in N-terminal extremity, it tends to cyclize during the chemical production
  • Avoid -DG- sequences
  • Shorter is better. Short sequences <20 amino acids are more easy to synthesize
  • Avoid oxidation-sensitive amino acids (Met, Cys, Trp). Met can eventually be replaced by Noreleucin, cystein by serine, tryptophane by lysine
  • Highly acid peptides can be capped in N-ter by acetyl group to gain a negative charge
  • Highly basic peptide can be amidated in C-ter to gain a positive charge