Related Experiment Video
Updated: Jun 4, 2025
Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Hemoglobin-derived amyloid fibrils: Fibrillization mechanisms and potential applications
Zerun Zhao1, Di Zhao1, Chunbao Li2
1State Key Laboratory of Meat Quality Control and Cultured Meat Development, MOST; Key Laboratory of Meat Processing, MARA; Jiangsu Innovative Center of Meat Production, Processing and Quality Control; College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, PR China.
Abstract:
Fibrils from food proteins were widely reported but it has not been reported on sus scrofa hemoglobin. Utilizing fibrillization strategies can efficiently utilize hemoglobin and reduce waste. This work explores a new strategy to prepare hemoglobin-derived fibrils by removing the heme group. Hydrophobic interaction was found to be a key factor in promoting the fibrillization process. Heme presence hindered the fibrillization process possibly by restricting the unfolding process due to its high hydrophobicity. The core sequences of fibrils were identified as HBA 30-36, HBA 96-110, HBA 126-139, HBB 15-41, HBB 104-117 and HBB 83-145, which are generally of high hydrophobicity and HSA (Hot spots of aggregation) scores. Fibrils exhibited excellent gel properties, water retention, iron-binding properties, and enhanced positive surface charge. These findings contribute to establishing a fibrillization mechanism of hemoglobin and highlight the possibility of hemoglobin-sourced fibrils in food industry.
More Related Videos
06:27Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
Published on: November 30, 2018
10:04Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
Published on: October 20, 2017
