Controlling Solvent Polarity to Regulate Protein Self-Assembly Morphology and Its Universal Insight for Fibrillation Mechanism-Reference-Cited by-同舟云学术

Controlling Solvent Polarity to Regulate Protein Self-Assembly Morphology and Its Universal Insight for Fibrillation Mechanism

Published:2024-03-28 Issue:14 Volume:40 Page:7733-7746
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Zhang Bao¹,Jiang Ruisheng¹,Dong Kexin¹,Li Jing¹,Zhang Yan¹²,Ghorani Behrouz³,Emadzadeh Bahareh³^ORCID,Nishinari Katsuyoshi¹²^ORCID,Yang Nan¹²^ORCID

Affiliation:

1. Glyn O. Phillips Hydrocolloid Research Centre, National “111″ Center for Cellular Regulation and Molecular Pharmaceutics, Key Laboratory of Fermentation Engineering of Ministry of Education, Key Laboratory of Industrial Microbiology in Hubei Province, Department of Bioengineering and Food Science, Hubei University of Technology, Wuhan 430068, China

2. Food Hydrocolloid International Science and Technology Cooperation Base of Hubei Province, Hubei University of Technology, Wuhan 430068, China

3. Department of Food Nanotechnology, Research Institute of Food Science & Technology (RIFST), Mashhad 91895-157-356, Iran

Funder

Department of Science and Technology of Hubei Province

Hubei University of Technology

Natural Science Foundation of Hubei Province

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.langmuir.4c00438

Reference58 articles.

1. Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications

2. Static and Dynamic Scattering of β-Lactoglobulin Aggregates Formed after Heat-Induced Denaturation at pH 2

3. Hydrophobicity-modulating self-assembled morphologies of α-zein in aqueous ethanol

4. Micrometer-Sized Fibrillar Protein Aggregates from Soy Glycinin and Soy Protein Isolate

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