Article
Biochemical Research Methods
Fatemeh Bardineshin, Seifollah Bahramikia, Reza Khodarahmi, Faranak Hadi
Summary: Mesalazine demonstrates inhibitory and destabilizing effects on human insulin fibrillation, suggesting its therapeutic potential in the treatment of insulin amyloidosis.
JOURNAL OF FLUORESCENCE
(2023)
Article
Biophysics
Victoria T. Reichelderfer, Andres F. Chaparro Sosa, Joel L. Kaar, Daniel K. Schwartz
Summary: The interactions between lipid bilayers and insulin can either stabilize or destabilize the protein, preventing or exacerbating the formation of amyloid fibrils.
COLLOIDS AND SURFACES B-BIOINTERFACES
(2022)
Article
Biochemistry & Molecular Biology
Hanna Nieznanska, Solomiia Boyko, Robert Dec, Maria Jolanta Redowicz, Wojciech Dzwolak, Krzysztof Nieznanski
Summary: The PKA-phosphorylated K18.280 oligomers are shown to be toxic to hippocampal neurons, leading to cell death, while the soluble N-terminal fragment N1 of prion protein (PrP) can protect neurons from the cytotoxic effects induced by these oligomers. These findings support the hypothesis on the neurotoxicity of Tau oligomers and the neuroprotective role of PrP-derived fragments in AD and other tauopathies, which could be valuable for the development of therapeutic strategies for these diseases.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
(2021)
Article
Biochemistry & Molecular Biology
Yang Gao, Stefan Wennmalm, Bengt Winblad, Sophia Schedin-Weiss, Lars O. Tjernberg
Summary: Through FRET imaging, Aβ42 oligomerization was successfully detected in primary neurons, showing that Aβ42 oligomerized in lysosomes/late endosomes in a concentration-dependent manner. These findings contribute to a better understanding of Aβ42 oligomerization in neurons.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Review
Biochemistry & Molecular Biology
Nicolas Papadopoulos, Nuria Suelves, Florian Perrin, Devkee M. Vadukul, Celine Vrancx, Stefan N. Constantinescu, Pascal Kienlen-Campard
Summary: Most neurodegenerative diseases are characterized by protein folding disorders, such as Alzheimer's disease. These diseases lead to the appearance of protein aggregates in vulnerable regions of the nervous system, which progressively spread through the neuronal network. Alzheimer's disease is characterized by neurofibrillary tangles composed of tau proteins and senile plaques composed of amyloid peptides. Understanding the structural determinants of the precursor protein APP and the formation of different A beta aggregates is crucial in deciphering the pathological conformational changes and mechanisms underlying amyloid fibril formation.
Article
Biology
Federica Pizzo, Maria Rosalia Mangione, Fabio Librizzi, Mauro Manno, Vincenzo Martorana, Rosina Noto, Silvia Vilasi
Summary: This study investigates the role of the heat shock protein cpn60/cpn10 in insulin assembly and pathological aggregation. The results show that these proteins assist in the formation of insulin hexamers and prevent aberrant aggregation. This provides new insights into insulin assembly and related disorders.
Article
Chemistry, Physical
Mohd Shahnawaz Khan, Faris Mohammad Alghadhiyyah, Mohammed Khaled Alhadeb, Yazeed Khalid Alhazzaa, Moneera Saud Al-Bagmi, Ghaliah S. Almutairi, Nojood Altwaijry, Majed S. Alokail
Summary: Protein aggregation occurs under abnormal conditions and can lead to deadly diseases. This study investigated the potential of hesperidin to inhibit the formation of insulin amyloid and found promising results.
JOURNAL OF MOLECULAR STRUCTURE
(2024)
Article
Biochemistry & Molecular Biology
Parastoo Shouhani, Seifollah Bahramikia, Seyed Hesamaldin Hejazi
Summary: This study investigated the anti-amyloidogenic and destabilizing effects of pyrogallol, a phenolic compound, on human insulin protein. The results showed that pyrogallol effectively reduced the formation of amyloid fibrils and caused shift in their position. This study has significant implications for the design of new anti-amyloid drugs in the future.
JOURNAL OF FOOD BIOCHEMISTRY
(2022)
Article
Biochemistry & Molecular Biology
Yu Zhang, Yuying Liu, Wenhui Zhao, Yunxiang Sun
Summary: The study demonstrates that SWCNT-OH has excellent anti-amyloid properties, inhibiting the fibrillization of beta 2m(21)(-)(31) peptides and destroying pre-formed proto-fibrils.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Review
Biochemistry & Molecular Biology
Anna Sulatskaya, Anastasiia O. Kosolapova, Alexander G. Bobylev, Mikhail Belousov, Kirill S. Antonets, Maksim Sulatsky, Irina M. Kuznetsova, Konstantin K. Turoverov, Olesya Stepanenko, Anton A. Nizhnikov
Summary: Both amyloids and beta-barrel proteins have beta-sheet-rich structures, with the latter being able to form functional amyloids in vivo. These beta-barrel amyloid proteins can interact with each other and form toxic oligomers, potentially contributing to the development of amyloidoses. Rapidly growing discoveries suggest that the number and diversity of functions of amyloid-forming beta-barrel proteins are significantly greater than currently understood.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Engineering, Chemical
Wei Liu, Xueting Sun, Xiaoyan Dong, Yan Sun
Summary: The chiral influence of peptide inhibitors on Aβ fibrillogenesis and cytotoxicity was investigated in this study. It was found that the D-enantiomer exhibited stronger inhibition effect on Aβ self-assembly compared to the L-enantiomer, with significant differences in their reaction.
CHINESE JOURNAL OF CHEMICAL ENGINEERING
(2022)
Article
Multidisciplinary Sciences
Takashi Ohgita, Hiroki Kono, Izumi Morita, Hiroyuki Oyama, Toshinori Shimanouchi, Norihiro Kobayashi, Hiroyuki Saito
Summary: Regulation of α-synuclein (αS) fibril formation is important for treating αS-related neurodegenerative disorders. Mouse αS forms fibrils faster than human αS due to the S87N substitution in the non-amyloid β component (NAC) region. Interaction of the C-terminal region with the N-terminal and NAC regions suppresses αS fibril formation, while the human-to-mouse S87N substitution accelerates fibril formation by perturbing intramolecular interaction.
SCIENTIFIC REPORTS
(2023)
Article
Immunology
Kyle M. Reid, Guy C. Brown
Summary: This study found that microglia release LRPAP1 when inflammatory activated or ER stressed. LRPAP1 can inhibit microglial phagocytosis, uptake of A beta, and A beta aggregation. Thus, the release of LRPAP1 may regulate microglial functions and A beta pathology.
FRONTIERS IN IMMUNOLOGY
(2023)
Review
Biochemical Research Methods
R. Prabakaran, Puneet Rawat, Sandeep Kumar, M. Michael Gromiha
Summary: This review provides a rigorous performance analysis of nine prediction tools for protein and peptide aggregation, revealing the robustness of current prediction tools and their potential for improvement. Insights gained from this work offer critical guidance to the scientific community on the advantages and limitations of different aggregation prediction methods.
BRIEFINGS IN BIOINFORMATICS
(2021)
Article
Biochemistry & Molecular Biology
Reito Nakamura, Ikumi Tomizawa, Atsushi Iwai, Tetsuo Ikeda, Kota Hirayama, Yung Wen Chiu, Takanobu Suzuki, Airi Tarutani, Tatsuo Mano, Atsushi Iwata, Tatsushi Toda, Youhei Sohma, Motomu Kanai, Yukiko Hori, Taisuke Tomita
Summary: Aggregation of alpha-synuclein into amyloid is a pathological hallmark of neurodegenerative disorders, and inhibiting this aggregation can be a potential therapeutic strategy. This study demonstrates that photo-oxygenation using a photocatalyst successfully inhibits alpha-synuclein aggregation by reducing its seeding ability. The oxidation of histidine residue in alpha-synuclein is found to be responsible for this inhibitory effect.