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Titleβ-Lactoglobulin Forms a Conserved Fibril Core That Assembles into Diverse Fibril Polymorphs.
Journal, issue, pagesNano Lett, Vol. 25, Issue 9, Page 3653-3661, Year 2025
Publish dateMar 5, 2025
AuthorsYongyi Xu / Danni Li / Yiling Zhang / Qinyue Zhao / Bo Sun / Cong Liu / Dan Li / Bin Dai /
PubMed AbstractThe β-lactoglobulin (β-LG) protein, sourced from dietary products, is notable for forming amyloid fibrils, which are increasingly recognized as valuable protein-based nanomaterials due to their ...The β-lactoglobulin (β-LG) protein, sourced from dietary products, is notable for forming amyloid fibrils, which are increasingly recognized as valuable protein-based nanomaterials due to their superior cytocompatibility, chemical resilience, and mechanical characteristics. However, the precise atomic details of β-LG's fibril assembly are not understood. In this study, we utilized cryo-electron microscopy to elucidate the composition and architecture of β-LG fibrils. We discovered that the β-LG fibril was rapidly assembled after a short time incubation. Remarkably, these fibril cores were composed of the first 32 residues, forming four β-strands that adopted a serpentine arrangement into a single protofilament. This protofilament core's stability was reinforced by hydrophobic interactions. Two identical protofilaments then align to form four distinct structural polymorphs through unique interfacial configurations, which were stabilized by hydrophilic interactions, hydrogen bonding, and electrostatic forces. Our findings provide a structural framework for understanding β-LG fibril formation and pave the way for designing innovative β-LG-based nanomaterials.
External linksNano Lett / PubMed:39992798
MethodsEM (helical sym.)
Resolution3.38 - 4.06 Å
Structure data

61480

9jhf

EMDB-61480, PDB-9jhf:
Cryo-EM structure of beta-LG fibril
Method: EM (helical sym.) / Resolution: 4.06 Å

61481

9jhg

EMDB-61481, PDB-9jhg:
Cryo-em structure of beta-LG fibril
Method: EM (helical sym.) / Resolution: 3.38 Å

61482

9jhh

EMDB-61482, PDB-9jhh:
Cryo-em structure of beta-LG fibril
Method: EM (helical sym.) / Resolution: 3.45 Å

61483

9jhi

EMDB-61483, PDB-9jhi:
Cryo-em structure of beta-LG fibril
Method: EM (helical sym.) / Resolution: 3.73 Å

Source
  • bos taurus (domestic cattle)
KeywordsPROTEIN FIBRIL / protein fribril / nanomaterials

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