Table 1_Licosin, a multifunctional defensin peptide originated from the clinical fungus Li

Licosin is a 41-residue defensin peptide identified from the clinical fungus Lichtheimia corymbifera. It exhibits antimicrobial activity against Gram-positive bacteria, including MRSA, and selectively inhibits the human potassium channel hKv1.3 with an IC50 of 0.4 μM. The dataset, authored by Weijia Chen and last updated in May 2026, comprises a DOCX file detailing its genomic, structural, and functional characterization.

Use Cases

• Identify novel antimicrobial peptide candidates based on the described activity against MRSA and Micrococcus luteus.
• Study structure-function relationships in defensins based on the described mature peptide sequence and disulfide bond formation.
• Screen for potassium ion channel blockers based on the described selective inhibition of hKv1.3.
• Investigate fungal defense mechanisms based on the characterization of a defensin from a clinical pathogen.

Strengths

• Includes specific IC50 value (0.4 ± 0.06 μM) for potassium channel inhibition.
• Provides detailed structural characterization, including mature peptide length (41 residues) and disulfide bond count (3).
• Data is openly licensed under CC-BY-4.0.

Limitations

• Dataset scope is limited to a single peptide; row count and column-level documentation are unknown.
• The primary data format is a DOCX document, which may require parsing to extract structured information.
• Freshness should be verified as the last update date is in the future (2026-05-11).

Provenance

Source

figshare

Collection Method

Characterization from genomic/mRNA sequences and LC-ESI-Q-TOF-MS/MS protein identification.

Freshness

Last updated 2026-05-11 04:29:27