Amyloid-like aggregation of recombinant β-lactoglobulin at pH 3.5 and 7.0: Is disulfide bond removal the key to fibrillation?-Reference-Cited by-同舟云学术

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Amyloid-like aggregation of recombinant β-lactoglobulin at pH 3.5 and 7.0: Is disulfide bond removal the key to fibrillation?

Published:2023-07 Issue: Volume:242 Page:124855
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Hoppenreijs Loes J.G.,Overbeck Achim,Brune Sarah E.,Biedendieck Rebekka,Kwade Arno,Krull Rainer,Boom Remko M.,Keppler Julia K.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference64 articles.

1. Engineering amyloid and amyloid-like morphologies of β-lactoglobulin;Hoppenreijs;Food Hydrocoll.,2022

2. Study of amyloid fibrils via atomic force microscopy;Adamcik;Curr Opin Colloid Interface Sci,2012

3. Protein fibrils from different food sources: a review of fibrillation conditions, properties, applications and research trends;Meng;Trends Food Sci. Technol.,2022

4. Protein oxidation during temperature-induced amyloid aggregation of beta-lactoglobulin;Keppler;Food Chem.,2019

5. Conformational prerequisites for α-lactalbumin fibrillation;Goers;Biochemistry,2002

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