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Updated: Jul 2, 2026

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
Published on: May 22, 2018
Cold plasma induced amyloid β-lactoglobulin fibrils-fucoidan self-assembled complexes for lycopene delivery:
Gongshuai Song1, Taijiao Xiang1, Haina Hou1
1Zhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, China.
Abstract:
In this study, a novel delivery system based on self-assembled complexes of amyloid beta-lactoglobulin fibrils (β-LGFs) and fucoidan (FD) was developed to encapsulate and protect lycopene in emulsions. β-LGFs were generated using a cold plasma (CP)-assisted acid-heat induction process under β-LG concentration of 10 mg/mL, CP treatment time of 80 s, and CP power of 60 W. Structural characterization of β-LGFs confirmed the formation of well-defined fibrils and their subsequent interaction with FD at pH 3.0 with a mass ratio of 3:1. The emulsions stabilized by the β-LGF-FD complex exhibited the superior thermal and ultraviolet stability of encapsulated lycopene. The highest retention rate (70.4 %) was obtained in the emulsion with 1.5 wt% β-LGF-FD complex and 50 % oil mass fraction after thermal treatment at 75 °C for 4 h. The increasing the concentration and oil mass fraction could promote the formation of a denser interface layer and more compact gel network structure.
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