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