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Supramolecular Assembly of Collagen-Mimetic Peptide D-Periodic Fibrils and Nanoassemblies

Cole, Carson C. ; Kreutzberger, Mark A.B. ; Klein, Kevin ; Cahue, Kiana A. ; Pogostin, Brett H. ; Farsheed, Adam C. ; Swain, Joseph W.R. ; Bui, Thi H. ; Dey, Arghadip and Makhoul, Jonathan T. , et al. (2026) In Biomacromolecules 27(4). p.2956-2965
Abstract

The collagen triple helix assembles hierarchically into bundled oligomers, solvated networks, and fibers. Synthetic peptide assemblies, driven by supramolecular interactions, can form single triple helices through intrahelical amino acid pairs; however, the principles guiding interhelical associations into higher-order structures remain unclear. Here, we incorporate cation−π and electrostatic charge pairs to probe interhelical interactions and elucidate the mechanisms driving triple helix assembly into fibrils, nanotubes, and nanosheets. Introducing cation−π pairs into a fibrillating collagen mimetic resulted in D-periodic fibrils with pH-sensitive gelation. By alternating the presentation of electrostatic and cation−π pairs, the... (More)

The collagen triple helix assembles hierarchically into bundled oligomers, solvated networks, and fibers. Synthetic peptide assemblies, driven by supramolecular interactions, can form single triple helices through intrahelical amino acid pairs; however, the principles guiding interhelical associations into higher-order structures remain unclear. Here, we incorporate cation−π and electrostatic charge pairs to probe interhelical interactions and elucidate the mechanisms driving triple helix assembly into fibrils, nanotubes, and nanosheets. Introducing cation−π pairs into a fibrillating collagen mimetic resulted in D-periodic fibrils with pH-sensitive gelation. By alternating the presentation of electrostatic and cation−π pairs, the assembly of another D-periodic fibril featuring inner and outer triple-helical layers was resolved by cryo electron microscopy to a resolution of 8 Å. At physiological pH, antiparallel association of these triple helices leads to the formation of nanotubes. The packing behavior of triple helices correlates with the interhelical interactions, where parallel associations favor fibril formation and antiparallel interactions drive nanotube and nanosheet assembly. These self-assembling triple-helical peptides demonstrate how packing of higher-order structures can be tailored with supramolecular interactions and establish the relationship of different hierarchical collagen-mimetic assemblies as pH-dependent.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biomacromolecules
volume
27
issue
4
pages
10 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:105035653597
  • pmid:41885220
ISSN
1525-7797
DOI
10.1021/acs.biomac.6c00345
language
English
LU publication?
yes
id
beb01259-a392-4aa2-8a1b-b2a8be31e705
date added to LUP
2026-05-26 11:28:50
date last changed
2026-05-27 03:00:06
@article{beb01259-a392-4aa2-8a1b-b2a8be31e705,
  abstract     = {{<p>The collagen triple helix assembles hierarchically into bundled oligomers, solvated networks, and fibers. Synthetic peptide assemblies, driven by supramolecular interactions, can form single triple helices through intrahelical amino acid pairs; however, the principles guiding interhelical associations into higher-order structures remain unclear. Here, we incorporate cation−π and electrostatic charge pairs to probe interhelical interactions and elucidate the mechanisms driving triple helix assembly into fibrils, nanotubes, and nanosheets. Introducing cation−π pairs into a fibrillating collagen mimetic resulted in D-periodic fibrils with pH-sensitive gelation. By alternating the presentation of electrostatic and cation−π pairs, the assembly of another D-periodic fibril featuring inner and outer triple-helical layers was resolved by cryo electron microscopy to a resolution of 8 Å. At physiological pH, antiparallel association of these triple helices leads to the formation of nanotubes. The packing behavior of triple helices correlates with the interhelical interactions, where parallel associations favor fibril formation and antiparallel interactions drive nanotube and nanosheet assembly. These self-assembling triple-helical peptides demonstrate how packing of higher-order structures can be tailored with supramolecular interactions and establish the relationship of different hierarchical collagen-mimetic assemblies as pH-dependent.</p>}},
  author       = {{Cole, Carson C. and Kreutzberger, Mark A.B. and Klein, Kevin and Cahue, Kiana A. and Pogostin, Brett H. and Farsheed, Adam C. and Swain, Joseph W.R. and Bui, Thi H. and Dey, Arghadip and Makhoul, Jonathan T. and Dubackic, Marija and Pal, Antara and Olsson, Ulf and Šarić, Anđela and Egelman, Edward H. and Hartgerink, Jeffrey D.}},
  issn         = {{1525-7797}},
  language     = {{eng}},
  number       = {{4}},
  pages        = {{2956--2965}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Biomacromolecules}},
  title        = {{Supramolecular Assembly of Collagen-Mimetic Peptide D-Periodic Fibrils and Nanoassemblies}},
  url          = {{http://dx.doi.org/10.1021/acs.biomac.6c00345}},
  doi          = {{10.1021/acs.biomac.6c00345}},
  volume       = {{27}},
  year         = {{2026}},
}