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Type: -
0 aa
Add Amino Acid
Cationic
Anionic
Hydrophobic
Polar
Physicochemical Parameters
Net Charge (> +2)
0
Hydrophobicity (-0.5 to +1.5)
0.00
Isoelectric Point (pI)
AMP: > 9.0
0.00
Hydrophobic Moment (μH)
Helix: > 0.50
0.00
Proteolytic Stability
Estimated: 0–100%
0%
CPP Potential (Cell Penetration Potential)
Predicted permeability through bacterial membranes: ≥ 50%
0%
Predicted Toxicity
The model assumes that a high content of hydrophobic residues (e.g., L, F) increases the risk of non-selective membrane disruption and hemolysis (lower % = better)
0%
Molar Mass:
0 Da
Amino Acid Composition
Helical Wheel
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Note: The visualization assumes the peptide adopts an ideal α-helix structure. Many AMPs adopt this structure only upon contact with a bacterial membrane.
