Table 3_Licosin, a multifunctional defensin peptide originated from the clinical fungus Li

A 41-residue mature defensin peptide named licosin was characterized from the clinical fungus Lichtheimia corymbifera. The peptide exhibits antimicrobial activity against gram-positive bacteria, including MRSA, and selectively inhibits the human potassium channel hKv1.3 with an IC50 of 0.4 ± 0.06 μM. Author Weijia Chen published this research data on figshare in May 2026 under a CC-BY-4.0 license.

Use Cases

• Screening for novel antimicrobial agents based on the described antibacterial activity against MRSA and Micrococcus luteus.
• Studying peptide-ion channel interactions based on the described dose-dependent inhibition of hKv1.3.
• Analyzing structure-function relationships in defensins based on the described 3D homology model and the role of lysine residues 34 and 35.

Strengths

• The mature peptide's amino acid sequence was identified at the protein level using LC-ESI-Q-TOF-MS/MS.
• The IC50 value for potassium channel inhibition is quantified at 0.4 ± 0.06 μM.
• The dataset is openly licensed under CC-BY-4.0.

Limitations

• The dataset is a 12.3 KB DOCX file, suggesting it contains descriptive text rather than structured data tables.
• 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 pathogen Lichtheimia corymbifera, involving genomic/mRNA sequence analysis, mass spectrometry, circular dichroism, and homology modeling.

Freshness

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