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Updated: Jan 13, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

加熱誘起型ミレットプロラミンの構造遷移と自己集合：マルチスケール構造解析

Liangxing Zhao¹, Luman Sang¹, Qingyu Zhao¹

¹College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China; National Grain Industry (Highland Barley Deep Processing) Technology Innovation Center, Beijing 100083, China; National Grain and Oil Standards Research Verification and Testing Center, Beijing 100083, China.

|January 10, 2026

Abstract:

Heat-induced structural transitions and assembly of millet prolamin (25-100 °C, 30 min) were profiled across scales. Differential scanning calorimetry revealed minimal thermal stability around 50 °C (peak temperature 65.7 °C; enthalpy change 114.6 J/g), consistent with a perturbed conformational state. At 70 °C, thermal parameters partially recovered and the particle size distribution narrowed, indicating a restructuring regime with strengthened intermolecular associations. At 90-100 °C, fibrillar aggregates formed, as evidenced by enhanced thioflavin T fluorescence, low polydispersity, increased zeta-potential magnitude and β-sheet enrichment in FT-IR spectra, while amino acid composition remained unchanged. Across these temperatures, aggregation was closely associated with hydrophobic interactions and hydrogen bonding. Overall, the data delineate three temperature-dependent structural regimes for millet prolamin-perturbation, restructuring and stabilization of compact aggregates-providing a practical framework for designing thermal processes to tailor the structure of plant proteins.

キーワード:

構造再構築熱誘起型タンパク質凝集ミレットプロラミンタンパク質自己集合熱安定性

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