Academic literature on the topic 'Β-lactoglobulin fibrils'
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Journal articles on the topic "Β-lactoglobulin fibrils"
Gowda, Vasantha, Michal Biler, Andrei Filippov, Malisa V. Mantonico, Eirini Ornithopoulou, Mathieu Linares, Oleg N. Antzutkin, and Christofer Lendel. "Structural characterisation of amyloid-like fibrils formed by an amyloidogenic peptide segment of β-lactoglobulin." RSC Advances 11, no. 45 (2021): 27868–79. http://dx.doi.org/10.1039/d1ra03575d.
Full textGosal, Walraj S., Simon B. Ross-Murphy, Paul D. A. Pudney, and Allan H. Clark. "Characterisation of amyloid fibrils formed from β-lactoglobulin." Biochemical Society Transactions 30, no. 3 (June 1, 2002): A83. http://dx.doi.org/10.1042/bst030a083.
Full textJones, Owen G., Stephan Handschin, Jozef Adamcik, Ludger Harnau, Sreenath Bolisetty, and Raffaele Mezzenga. "Complexation of β-Lactoglobulin Fibrils and Sulfated Polysaccharides." Biomacromolecules 12, no. 8 (August 8, 2011): 3056–65. http://dx.doi.org/10.1021/bm200686r.
Full textArnaudov, Luben N., Renko de Vries, Hans Ippel, and Carlo P. M. van Mierlo. "Multiple Steps during the Formation of β-Lactoglobulin Fibrils." Biomacromolecules 4, no. 6 (November 2003): 1614–22. http://dx.doi.org/10.1021/bm034096b.
Full textRabe, Rebecca, Ute Hempel, Laurine Martocq, Julia K. Keppler, Jenny Aveyard, and Timothy E. L. Douglas. "Dairy-Inspired Coatings for Bone Implants from Whey Protein Isolate-Derived Self-Assembled Fibrils." International Journal of Molecular Sciences 21, no. 15 (August 3, 2020): 5544. http://dx.doi.org/10.3390/ijms21155544.
Full textMa, Baoliang, Wen Li, Xudong Zhu, Guiling Liu, Fan Zhang, Fang Wu, Xiping Jiang, and Jinbing Xie. "Folic acid inhibits the amyloid fibrils formation of β-lactoglobulin." European Journal of BioMedical Research 1, no. 1 (February 10, 2017): 22. http://dx.doi.org/10.18088/ejbmr.1.1.2015.pp22-27.
Full textChen, Da, Lorena Silva Pinho, Enrico Federici, Xiaobing Zuo, Jan Ilavsky, Ivan Kuzmenko, Zhi Yang, Owen Griffith Jones, and Osvaldo Campanella. "Heat accelerates degradation of β-lactoglobulin fibrils at neutral pH." Food Hydrocolloids 124 (March 2022): 107291. http://dx.doi.org/10.1016/j.foodhyd.2021.107291.
Full textDunstan, Dave E., Paul Hamilton-Brown, Peter Asimakis, William Ducker, and Joseph Bertolini. "Shear-induced structure and mechanics of β-lactoglobulin amyloid fibrils." Soft Matter 5, no. 24 (2009): 5020. http://dx.doi.org/10.1039/b914089a.
Full textPeng, Dengfeng, Jinchu Yang, Jing Li, Cuie Tang, and Bin Li. "Foams Stabilized by β-Lactoglobulin Amyloid Fibrils: Effect of pH." Journal of Agricultural and Food Chemistry 65, no. 48 (November 28, 2017): 10658–65. http://dx.doi.org/10.1021/acs.jafc.7b03669.
Full textAkkermans, Cynthia, Paul Venema, Atze Jan van der Goot, Remko M. Boom, and Erik van der Linden. "Enzyme-Induced Formation of β-Lactoglobulin Fibrils by AspN Endoproteinase." Food Biophysics 3, no. 4 (August 13, 2008): 390–94. http://dx.doi.org/10.1007/s11483-008-9094-3.
Full textDissertations / Theses on the topic "Β-lactoglobulin fibrils"
Lin, Chien-Yu, and 林千鈺. "Examining the Effects of Sugar-Terminated Nanoparticles on Amyloid Fibril Formation of β-Lactoglobulin." Thesis, 2019. http://ndltd.ncl.edu.tw/handle/r3r4z6.
Full text國立臺灣大學
化學工程學研究所
107
Currently, accumulation of proteins/peptides has been found to be associated with many diseases, such as Alzheimer''s disease, Parkinson''s disease, and Huntington''s disease. It has been shown that the addition of small molecules or nanoparticles can interfere with amyloid fibril formation. In this study, β-lactoglobulin (β-LG) was used to form amyloid fibrils under high temperature and acidic conditions. Although the protein itself is not pathogenic, understanding the behavior and characteristics of its amyloid aggregation form could provide a better understanding of how inhibitors affect protein fibrillogenesis. Moreover, the knowledge gained here could also aid in designing new inhibitory molecules. Herein, the sugar (sucrose or fructose)-terminated nanoparticles were used as the protein aggregation inhibitors. Our results showed that both sucrose and fructose nanoparticles could significantly retard and/or decrease β-LG fibrillation. In addition, results showed that the secondary structure of β-LG was stabilized in the presence of the sugar-based nanoparticles under 80˚C and pH 2.0 conditions. However, this secondary structural stabilization behavior was not observed when the two sugars in their molecular form were added. Using ANS binding assay, we found that the sugar-terminated nanoparticles effectively reduced the degree of exposure of the β-LG hydrophobic area. Furthermore, as revealed by light scattering experiment and electrophoresis, the size of aggregates was observed to significantly decrease as the sugar nanoparticles at higher concentrations were added. We also went ahead to analyze the interaction/binding between sugar nanoparticles and β-LG by fluorescence quenching experiments at different temperatures. Several points could be made from the fluorescence quenching results: (1) The reaction between proteins and sugar terminated nanoparticles was determined to be exothermic. (2) Hydrogen bonding may play an important role in the interaction between protein and nanoparticles. (3) The binding constants of the fructose nanoparticle group at three temperatures were all considerably higher than those of the sucrose nanoparticle system, implying that the interaction between fructose nanoparticles and β-LG was favorable or β-LG has a high affinity for fructose nanoparticles. As revealed by several spectroscopic tools and biophysical methods, the sucrose and fructose-terminated nanoparticles synthesized in this study were found to be more effective in inhibiting β-LG fibril formation, as compared to their molecular form., This result suggested that the sugar nanoparticle structure could provide multivalent bonds, thereby reducing the formation of β-LG amyloid fibrils. While more research is warranted to decipher the underlying mechanism of action of sugar-based nanoparticles against protein fibril formation, we believe the outcome from this work may aid in the development of potential inhibitory agents against the diseases associated with amyloid fibrillogenesis.
Book chapters on the topic "Β-lactoglobulin fibrils"
van den Akker, Corianne C., Michael Schleeger, Mischa Bonn, and Gijsje H. Koenderink. "Structural Basis for the Polymorphism of β-Lactoglobulin Amyloid-Like Fibrils." In Bio-nanoimaging, 333–43. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-394431-3.00031-6.
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