9IAH

Structure of beta-lactoglobulin fibril

9IAH の概要

• エントリーDOI: 10.2210/pdb9iah/pdb
• EMDBエントリー: 52781
• 分子名称: Beta-lactoglobulin (1 entity in total)
• 機能のキーワード: whey protein, nutrient transport, amyloid fibrillation, cross-beta structure, nanomaterial, biosynthetic protein
• 由来する生物種: Bos taurus (domestic cattle)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 18136.16

構造登録者

Sternke-Hoffmann, R.,Rhyner, D.,Qureshi, B.,Riek, R.,Greenwald, J.,Luo, J. (登録日: 2025-02-10, 公開日: 2025-03-05, 最終更新日: 2025-11-26)

主引用文献

Sternke-Hoffmann, R.,Rhyner, D.,Terashi, G.,Qureshi, B.M.,Riek, R.,Greenwald, J.,Kihara, D.,Lutz-Bueno, V.,Luo, J.
Structural Insights and Functional Dynamics of beta-Lactoglobulin Fibrils.
Nano Lett., 25:16146-16153, 2025

PubMed Abstract: Amyloid fibrils from β-lactoglobulin (β-LG), a major whey protein, have attracted interest for nanotechnology due to their biocompatibility, tunable surface chemistry, and ability to bind functional molecules. They serve as scaffolds for metal nanoparticle synthesis, carriers for bioactive compounds, and building blocks for nanomaterials with tailored mechanical and optical properties. However, their dynamic architecture remains incompletely understood, limiting their rational design. Here, we combine cryo-electron microscopy (cryo-EM), small-angle X-ray scattering (SAXS), and molecular dynamics (MD) simulations to investigate β-LG fibrils formed under mildly denaturing conditions. Cryo-EM reveals a monomeric polymorph with a conserved core (Leu1-Ala34) and a disordered "fuzzy coat". Flexible domains were modeled and evaluated by MD, identifying one stable conformation (Asn90-Thr97). The ionic strength reduced the coat flexibility and promoted iron binding, suggesting environmental responsiveness. These findings link fibril flexibility to functional potential, offering mechanistic insight into engineering β-LG-based nanomaterials.

PubMed: 41129746
DOI: 10.1021/acs.nanolett.5c04125

実験手法

ELECTRON MICROSCOPY (3.17 Å)