9HGB

Amyloid fibril from the antimicrobial peptide citropin 1-3 - Polymorph Nr.3

Summary for 9HGB

• Entry DOI: 10.2210/pdb9hgb/pdb
• EMDB information: 52133
• Descriptor: Citropin-1.3 (1 entity in total)
• Functional Keywords: amyloid helical, antimicrobial protein
• Biological source: Ranoidea citropa (Blue Mountains treefrog)
• Total number of polymer chains: 12
• Total formula weight: 19583.98

Authors

Strati, F.,Rayan, B.,Landau, M.,Siavash, M.,Cali, P.M.,Monistrol, J.,Golubev, A.,Gustavsson, E.,Bloch, Y. (deposition date: 2024-11-19, release date: 2025-10-01, Last modification date: 2026-04-15)

Primary citation

Strati, F.,Cali, M.P.,Bloch, Y.,Mostafavi, S.,Monistrol, J.,Golubev, A.,Rayan, B.,Gustavsson, E.,Landau, M.
Structural and Functional Versatility of the Amyloidogenic Non-Amidated Variant of the Antimicrobial Peptide Citropin 1.3.
Adv Sci, 12:e03997-e03997, 2025

PubMed Abstract: Citropin 1.3 is an antimicrobial peptide secreted by the amphibian Litoria citropa (Southern bell frog). In this study, the structural and functional properties of its non-amidated form, which self-assembles into distinct fibrillar architectures, are investigated. Using cryogenic electron microscopy, X-ray crystallography, and fluorescence microscopy with model membranes and cells, diverse supramolecular structures, including canonical amyloid fibrils, multilayered nanotubes, and a novel mixed fibril type, are identified. In giant unilamellar vesicles, citropin 1.3 promoted membrane fusion and underwent lipid-induced phase separation. In mammalian cells, it permeabilized membranes, induced cell death, and colocalized with nucleic acids. These findings link antimicrobial activity to amyloid assembly and highlight the peptide's structural plasticity and potential biological functions, offering new insights into amyloid-based antimicrobial mechanisms.

PubMed: 41016026
DOI: 10.1002/advs.202503997

Experimental method

ELECTRON MICROSCOPY (3.1 Å)