Table 2_Licosin, a multifunctional defensin peptide originated from the clinical fungus Li

A new fungal defensin peptide named licosin was characterized from the clinical pathogen Lichtheimia corymbifera. The dataset includes its genomic and cDNA sequence, amino acid structure, and results from antimicrobial and ion channel blocking assays. The data was authored by Weijia Chen and last updated on May 11, 2026.

Use Cases

• Identify novel antimicrobial peptide candidates based on the characterized sequence and activity against MRSA.
• Study structure-function relationships in toxin-like defensins based on the described amino acid sequence and disulfide bond pattern.
• Screen for potassium channel (hKv1.3) inhibitors based on the reported IC50 value and key lysine residues.
• Investigate the innate immune components of pathogenic fungi based on the defensin characterization.

Strengths

• Includes specific quantitative results, such as an IC50 value of 0.4 ± 0.06 μM for hKv1.3 channel inhibition.
• Provides detailed structural characterization, including a 207 bp cDNA sequence and a mature peptide of 41 residues.
• Data is openly licensed under CC-BY-4.0.

Limitations

• Dataset is very small (12.1 KB), suggesting limited scope, likely a single research document.
• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.

Provenance

Source

figshare

Collection Method

Characterization from the clinical fungus Lichtheimia corymbifera, involving genomic analysis, LC-ESI-Q-TOF-MS/MS, and bioassays.

Freshness

Last updated 2026-05-11 04:29:33; freshness should be verified.