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Malacidin A, along with Malacidin B, is a member of a class of chemicals made by bacteria found in soil that can kill Gram-positive bacteria . Malacidins are 10-member macrocycle lipopeptides discovered via gene sequencing and bioinformatic analysis. While structurally similar to other macrocycle drugs like Daptomycin and Friulimicin B, Malacidin A appears to act via its own distinct mechanism.
Malacidin A, along with Malacidin B, is a member of a class of chemicals made by bacteria found in soil that can kill Gram-positive bacteria . Malacidins are 10-member macrocycle lipopeptides discovered via gene sequencing and bioinformatic analysis. While structurally similar to other macrocycle drugs like Daptomycin and Friulimicin B, Malacidin A appears to act via its own distinct mechanism.
Malacidin A appears to bind Lipid II via a calcium dependent mechanism despite the absence of the typical Asp-X-Asp-Gly motif associate with calcium binding. The structure of Malacidin A includes a 3-hydroxy-aspartate residue while the "X" variable spacer residue is absent. It is unknown how these unique structural features may impact the drug's mechanism of action. The binding of Malacidin A to Lipid II prevents the incorporation of the subunit into the cell wall, disrupting synthesis and likely resulting in death of the bacterial cell. Malacidin A does not appear to form pores nor does it seem to integrate into the cell wall. While this mechanism is similar to that of Vancomycin, Malacidin A retains its activity against Vancomycin-resistant pathogens. Unlike other antibiotic agents, Malacidin A also retains its activity in the presence of pulmonary surfactants.
Malacidin A is being investigated for its antibiotic action and has potential for use as an antibacterial agent in the future .
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