Amyloids and Amyloid-like Protein Aggregates in Foods: Challenges and New Perspectives

被引:3
|
作者
Malik, Shweta [1 ]
Yadav, Jay Kant [1 ]
机构
[1] Cent Univ Rajasthan, Dept Biotechnol, NH 8 Bandar Sindri, Ajmer 305817, Rajasthan, India
关键词
Protein misfolding; food-derived amyloids; human intestine; protein aggregation; gut microbiome; Alzheimer's diseases; INTERFACIAL RHEOLOGICAL PROPERTIES; BETA-LACTOGLOBULIN; FIBRIL FORMATION; EGG-WHITE; INDUCED GELATION; AA AMYLOIDOSIS; PEPTIDE; WHEY; MILK; SOY;
D O I
10.2174/1389203724666230104163924
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein misfolding and amyloid formations are associated with many neurodegenerative and systemic diseases. The discovery of Alzheimer's disease and its association with the accumulation of Amyloid-& beta; (A & beta;) peptides in the plaques uncovered the pleiotropic nature of peptides/ proteins. As of today, more than 50 proteins/ peptides are reported to form amyloids or amyloid-like protein aggregates under different conditions, establishing that amyloid formation could be a generic property of many proteins. In principle, under certain conditions, all the proteins have this property to form amyloid-like aggregates, which can be toxic or non-toxic. The extensive research in this direction led to an understanding of the ubiquitous nature of amyloids. Mounting evidences suggest that processed foods, particularly protein-rich foods, could be a plethora of amyloids or amyloid-like protein aggregates. Many are reported to be toxic, and their consumption raises health concerns. The assimilation of dietary proteins in the human body largely depends upon their conformational states and the digestive integrity of the gastrointestinal system. Amyloids or amyloid-like protein aggregates are usually protease resistant, and their presence in foods is likely to reduce nutritional value. Several biochemical and biophysical factors, commonly evident in various food processing industries, such as high temperature, the addition of acid, etc., are likely to induce the formation of protease-resistant protein aggregates. Aging significantly alters gastrointestinal health, predisposing aged individuals to be more susceptible to protein aggregation-related diseases. Consumption of foods containing such protein aggregates will lead to a poor supply of essential amino acids and might exaggerate the amyloid-related disease etiology. On the other hand, the gut microbiome plays a crucial role during pathological events leading to the development of Alzheimer's and Parkinson's diseases. The activity of gastrointestinal proteases, pH change, gut microbiome, and intestinal epithelium integrity would largely determine the outcome of consuming foods loaded with such protein aggregates. The current review outlines the recent development in this area and a new perspective for designing safe protein-rich diets for healthy nutrition.
引用
收藏
页码:393 / 403
页数:11
相关论文
共 50 条
  • [21] Isolation and characterization of amyloid-like protein aggregates from soya beans and the effect of low pH and heat treatment on their stability
    Jangir, Neelam
    Bangrawa, Shreya
    Yadav, Tamanna
    Malik, Shweta
    Alamri, Abdulhakeem S.
    Galanakis, Charis M.
    Singh, Manish
    Yadav, Jay Kant
    JOURNAL OF FOOD BIOCHEMISTRY, 2022, 46 (10)
  • [22] Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli
    Navarro, Susanna
    Ventura, Salvador
    BIOTECHNOLOGY JOURNAL, 2014, 9 (10) : 1259 - 1266
  • [23] Members of the GADD45 Protein Family Show Distinct Propensities to form Toxic Amyloid-Like Aggregates in Physiological Conditions
    Smaldone, Giovanni
    Caruso, Daniela
    Sandomenico, Annamaria
    Iaccarino, Emanuela
    Foca, Annalia
    Ruggiero, Alessia
    Ruvo, Menotti
    Vitagliano, Luigi
    INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2021, 22 (19)
  • [24] Distribution of Amyloid-Like and Oligomeric Species from Protein Aggregation Kinetics
    Silva, Alexandra
    Almeida, Bruno
    Fraga, Joana S.
    Taboada, Pablo
    Martins, Pedro M.
    Macedo-Ribeiro, Sandra
    ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2017, 56 (45) : 14042 - 14045
  • [25] Tuning protein assembly pathways through superfast amyloid-like aggregation
    Li, Chen
    Xu, Lu
    Zuo, Yi Y.
    Yang, Peng
    BIOMATERIALS SCIENCE, 2018, 6 (04) : 836 - 841
  • [26] Formation of pea protein amyloid-like nanofibrils-derived hydrogels mediated by epigallocatechin gallate
    Zhang, Hailing
    Kang, Ling
    Bhutto, Rizwan Ahmed
    Fan, Yuting
    Yi, Jiang
    FOOD CHEMISTRY, 2024, 459
  • [27] Amyloid-Like Fibril Formation by Tachykinin Neuropeptides and Its Relevance to Amyloid β-Protein Aggregation and Toxicity
    Pradeep K. Singh
    Samir K. Maji
    Cell Biochemistry and Biophysics, 2012, 64 : 29 - 44
  • [28] Amyloid-Like Fibril Formation by Tachykinin Neuropeptides and Its Relevance to Amyloid β-Protein Aggregation and Toxicity
    Singh, Pradeep K.
    Maji, Samir K.
    CELL BIOCHEMISTRY AND BIOPHYSICS, 2012, 64 (01) : 29 - 44
  • [29] Formation of amyloid-like aggregates through the attachment of protein molecules to a Congo red scaffolding framework ordered under the influence of an electric field
    Stopa, Barbara
    Piekarska, Barbara
    Konieczny, Leszek
    Krol, Marcin
    Rybarska, Janina
    Jagusiak, Anna
    Spolnik, Pawel
    Roterman, Irena
    Urbanowicz, Barbara
    Piwowar, Piotr
    Lewinski, Krzysztof
    CENTRAL EUROPEAN JOURNAL OF CHEMISTRY, 2010, 8 (01): : 41 - 50
  • [30] Amyloid-like aggregation of bovine serum albumin at physiological temperature induced by cross-seeding effect of HEWL amyloid aggregates
    Nirwal, Sadhana
    Bharathi, Vidhya
    Patel, Basant K.
    BIOPHYSICAL CHEMISTRY, 2021, 278