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1.D.118. The Pore-forming B18 Peptide derived from the B49Mod1 Protein (B49-B18) Family

Inhibition of cancer cell adhesion is an effective approach to killing adherent cancer cells. B49 and its analog B49Mod1 peptides, derived from the extracellular domain (ECD) of bone marrow stromal antigen 2 (BST-2), display anti-adhesion activity on breast cancer cells.  Lyu et al. 2020 characterized the anti-adhesion activity of B49Mod1 and showed that the anti-adhesion activity of B49Mod1 requires a cysteine-disulfide bond, and that the peptide is susceptible to proteolytic deactivation. They identified an 18-Mer sequence (B18) as the minimal peptide sequence mediating the anti-adhesion activity of B49Mod1. Atomistic molecular dynamic (MD) simulations reveal that B18 forms a stable complex with the ECD of BST-2 in aqueous solution and revealed that B18 may cause membrane defects that facilitate peptide translocation across the bilayer. Placement of four B18 chains as a transmembrane bundle resulted in water channel formation, indicating that B18 may impair membrane integrity and form pores (Lyu et al. 2020).The sequence of the 18 aa pore-forming peptide is: GFQDVEAQAATCNHTVMA.

References associated with 1.D.118 family:

Lyu, Y., W.D. Mahauad-Fernandez, and C.M. Okeoma. (2020). Development and Characterization of the Shortest Anti-Adhesion Peptide Analogue of B49Mod1. Molecules 25:. 32155736