Pradimicin A 

Pradimicin A is a potent antifungal agent with a minimum inhibitory concentration (MIC) of 4 μg/mL against Candida rugosa. Pradimicin A exhibits antiviral activity against SARS-CoV, human immunodeficiency virus (HIV) and other enveloped viruses. Pradimicin A exerts its fungicidal activity through a Ca²⁺-dependent mechanism, which induces fungal lysis. Pradimicin A can be used in research related to fungal infections, HIV infections and COVID-19^{[1][2][3][4][5]}.

Pradimicin A (48 h) inhibits the growth of Candida rugosa with a minimum inhibitory concentration (MIC) of 4 μg/mL, and completely inhibits Candida rugosa growth while showing preferential binding to branched oligomannose motifs 6 and 7 (MAC = 1 mM) relative to other tested glycan structures^[1][3].
Pradimicin A (0.3-100 μM; 1 h pre-incubation, 3 days post challenge) inhibits SARS-CoV-2 infection of Calu-3 cells with an IC₅₀ of 1.2 μM, shows no cytotoxicity at concentrations up to 100 μM, and its antiviral activity is dependent on binding to branched oligomannose motifs on viral spike proteins^[1].
Pradimicin A (1 mM) shows Ca²⁺‑dependent specific binding to Man-OMe (100 mM) with two distinct binding sites in ITC assays (40 injections, 30 °C). The primary binding (K_a = 10400 M⁻¹) is approximately 40‑fold stronger than the secondary binding (K_a = 263 M⁻¹)^[2].
Pradimicin A (1 mM) binds methyl α-D-mannopyranoside in a cell-free buffer system with a primary dissociation constant (K_d1) of 96 μM and a secondary dissociation constant (K_d2) of 3800 μM^[3].
Pradimicin A (0.8-12.5 μg/mL) exhibits broad-spectrum antifungal activity against diverse fungal species including Candida albicans A9540^[5].
Pradimicin A exhibits antiviral activity against coronaviruses and HIV-1, targeting viral glycoprotein mannose moieties and demonstrating a high genetic barrier to HIV-1 resistance^[5].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

840.78

C₄₀H₄₄N₂O₁₈

117704-65-1

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Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Nakagawa Y, et al. Molecular basis of N-glycan recognition by pradimicin a and its potential as a SARS-CoV-2 entry inhibitor. Bioorg Med Chem. 2024 May 1;105:117732.

  [2]. Nakagawa Y, et al. Mapping of the primary mannose binding site of pradimicin A. J Am Chem Soc. 2011;133(43):17485-17493.  [Content Brief]

  [3]. Miyanishi W, et al. d-Mannose binding, aggregation property, and antifungal activity of amide derivatives of pradimicin A. Bioorg Med Chem. 2022;55:116590.  [Content Brief]

  [4]. Nakagawa Y, et al. Molecular Basis of Mannose Recognition by Pradimicins and their Application to Microbial Cell Surface Imaging. Cell Chem Biol. 2019;26(7):950-959.e8.

  [5]. Guo Y, et al. Isolation, biosynthesis, and biological activity of pradimicins from actinomycetes. Bioorg Chem. 2025;164:108884.