9O7L

Cryo-EM of pi-conjugated Peptide 2 (6 strands)

This is a non-PDB format compatible entry.

Summary for 9O7L

• Entry DOI: 10.2210/pdb9o7l/pdb
• EMDB information: 70203
• Descriptor: pi-conjugated peptide, 2,2'-[thiophene-2,5-diyldi(4,1-phenylene)]diacetic acid (2 entities in total)
• Functional Keywords: peptide fiber, helical polymer, protein fibril
• Biological source: synthetic construct
• Total number of polymer chains: 6
• Total formula weight: 3898.33

Authors

Rich-New, S.T.,Wang, R.,Zia, A.,Tovar, J.D.,Wang, F. (deposition date: 2025-04-15, release date: 2025-07-30, Last modification date: 2025-09-03)

Primary citation

Rich-New, S.T.,Wang, R.,Zia, A.,Wang, F.,Tovar, J.D.
Cryo-EM Visualization of Intermolecular pi-Electron Interactions within pi-Conjugated Peptidic Supramolecular Polymers.
ACS Macro Lett, 14:1100-1106, 2025

PubMed Abstract: The self-assembly of "π-peptides" - molecules with π-electron cores substituted with two or more oligopeptide chains - brings organic electronic function into biologically relevant nanomaterials. π-Peptides assemble into fibrillar nanomaterials as driven by enthalpic peptide-based hydrogen bonding networks and pi-core-based quadrupolar interactions. A large body of spectroscopic, morphological and computational studies informs on the nature of the self-assembly process and the resulting nanostructures, but detailed structural information has remained elusive. Inspired by the recent use of cryogenic electron microscopy (cryo-EM) to provide high-resolution structures for synthetic peptide nanomaterials, we present here the use of cryo-EM to offer ca. 3 Å resolution of π-peptide nanomaterial assemblies, visualizing for the first time the nature of the intermolecular π-core electronic interactions responsible for energy transport through these supramolecular materials.

PubMed: 40686463
DOI: 10.1021/acsmacrolett.5c00360

Experimental method

ELECTRON MICROSCOPY (3.2 Å)