Tilted Peptides are short motifs of proteins (12 to 18 residues) involved in the destabilization of hydrophobicity interfaces during the fusion of membranes (fusion of viruses to their hosts), during the extraction of lipids from membranes or lipid aggregates (lipases) and probably during the destabilization of proteins (amyloid formation). Unlike most motifs of proteins, Tilted peptides are not conserved residues, but are a conserved tilted hydrophobicity gradient in a short helix fragment. This hydrophobicity gradient is responsible for the functional destabilizing properties.

We can analyze protein sequences to predict which fragments are tilted peptides and, to propose mutations to experimentally inactivate the tilted peptides and hence validate its role.