Article
Biochemistry & Molecular Biology
Axell Rodriguez, Abid Ali, Aidan P. Holman, Tianyi Dou, Kiryl Zhaliazka, Dmitry Kurouski
Summary: Transthyretin (TTR) amyloidosis is a progressive disease characterized by the abrupt aggregation of misfolded protein in multiple organs and tissues. The structural organization of TTR oligomers during protein aggregation has been investigated using nano-infrared spectroscopy (AFM-IR). Two types of TTR oligomers were identified, with Type 1 being non-toxic and dominated by alpha-helix and beta-sheet structures, while Type 2 oligomers appeared at a later stage and were primarily composed of beta-sheet structures.
Article
Biochemistry & Molecular Biology
Kiryl Zhaliazka, Dmitry Kurouski
Summary: The aggregation of misfolded proteins is a key factor in Alzheimer's disease and Parkinson's disease, both of which are severe pathologies affecting millions of people worldwide. A study using nano-Infrared imaging technique investigated the structural organization of amyloid beta and alpha-synuclein fibrils in the brains of AD and PD patients. The researchers observed two different morphologically fibril polymorphs in each patient's brain, as well as the presence of lipids in the structure of alpha-synuclein fibrils, suggesting a potential role of lipid membranes in the onset and progression of PD.
Article
Biochemistry & Molecular Biology
Kiryl Zhaliazka, Mikhail Matveyenka, Dmitry Kurouski
Summary: Abrupt aggregation of amyloid beta(1-42) (Aβ) peptide is a hallmark of Alzheimer's disease (AD), and lipids have been found to uniquely alter the rate and structure of Aβ(1-42) aggregation. In this study, the effect of phosphatidylcholine (PC), cardiolipin (CL), and cholesterol (Chol) on Aβ(1-42) aggregation was investigated. The results showed that these lipids significantly accelerated the rate of fibril formation and modified the secondary structure of Aβ(1-42) aggregates.
Article
Biochemistry & Molecular Biology
Mikhail Matveyenka, Kiryl Zhaliazka, Dmitry Kurouski
Summary: Phosphatidylserine (PS), a negatively charged lipid, plays a critical role in cell apoptosis. Decreased ATP levels in cells lead to an increase in PS concentration on the outer membranes, activating phagocytes and triggering cell apoptosis. In this study, the effects of PS concentration on protein aggregation and secondary structure were investigated. The results showed that increased PS concentration caused a significant increase in insulin aggregation and altered the toxicities of protein aggregates.
ACS CHEMICAL NEUROSCIENCE
(2023)
Article
Biochemistry & Molecular Biology
Abid Ali, Kiryl Zhaliazka, Tianyi Dou, Aidan P. Holman, Dmitry Kurouski
Summary: This study investigates the impact of phosphatidylserine (PS) on the stability of transthyretin (TTR) and found that all analyzed lipids can slow down the aggregation rate of TTR. Furthermore, the length and saturation of fatty acids in PS also alter the morphology and secondary structure of TTR aggregates. Consequently, TTR fibrils formed in the presence of specific fatty acids in PS exhibit significantly lower cell toxicity.
ACS CHEMICAL NEUROSCIENCE
(2023)
Article
Biochemistry & Molecular Biology
Zigmantas Toleikis, Mantas Ziaunys, Lina Baranauskiene, Vytautas Petrauskas, Kristaps Jaudzems, Vytautas Smirnovas
Summary: The presence of S100A9 alters the aggregation kinetics of alpha-synuclein and stabilizes a specific amyloid fibril structure. The ionic strength of the solution influences the interaction between S100A9 and alpha-synuclein, stabilizing a different structure of alpha-synuclein fibrils.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Biochemistry & Molecular Biology
Aruna K. Mora, Sushant Murudkar, Neelam Shivran, Soumyaditya Mula, Subrata Chattopadhyay, Sukhendu Nath
Summary: Protein oligomers, formed under physiological stress, are neurotoxic and linked to neurological diseases. Early detection is crucial, and a new NIR-emitting fluorescent probe has been developed for this purpose. The probe not only detects matured fibrils but also probes oligomer formation, showing potential for in vivo imaging.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Article
Biochemistry & Molecular Biology
Abid Ali, Kiryl Zhaliazka, Tianyi Dou, Aidan P. Holman, Dmitry Kurouski
Summary: This study investigated the effect of phosphatidic acid (PA) on the aggregation of transthyretin (TTR). The results showed that PAs with different length and saturation of fatty acids (FAs) led to different structural and morphological properties of TTR aggregates, and PAs significantly reduced the toxicity of TTR aggregates. These findings shed light on the role of PA in TTR stability and transthyretin amyloidosis.
CHEMISTRY AND PHYSICS OF LIPIDS
(2023)
Article
Biochemistry & Molecular Biology
Addison Frese, Cody Goode, Kiryl Zhaliazka, Aidan P. Holman, Tianyi Dou, Dmitry Kurouski
Summary: The aggregation of misfolded proteins is the fundamental molecular cause of severe pathologies such as Alzheimer's and Parkinson's diseases. Lipids are found to play a vital role in this process. In this study, the researchers investigated the impact of the length and saturation of fatty acids in phosphatidylserine (PS) on lysozyme aggregation. The results showed that both factors influenced the aggregation rate of insulin. The presence of double bonds in fatty acids accelerated the rate of insulin aggregation relative to PS with fully saturated fatty acids.
Article
Biochemistry & Molecular Biology
Kiryl Zhaliazka, Dmitry Kurouski
Summary: In this study, AFM-IR spectroscopy was used to investigate the secondary structure changes of A β peptide during aggregation. It was found that at the early stage, parallel β-sheet oligomers dominated, while antiparallel β-sheet oligomers appeared in the middle stage and coexisted with the parallel β-sheet fibrils at the late stage.
ACS CHEMICAL NEUROSCIENCE
(2022)
Review
Biochemistry & Molecular Biology
Parveen Salahuddin, Munazza Tamkeen Fatima, Vladimir N. Uversky, Rizwan Hasan Khan, Zeyaul Islam, Mohammad Furkan
Summary: Neurodegenerative diseases are characterized by the abnormal loss of neurons, with common pathogenic mechanisms involving misfolding and aggregation of proteins. Accumulating evidence suggests that amyloid oligomers, not fibrils, are the most toxic species causing AD and PD.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Article
Biochemistry & Molecular Biology
Qize Xuan, Jiaxin He, Wenxue Zhang, Wei Zhang, Qi Zhang, Yao Zhou, Anqi Wei, Hao Wang, Hui Li, Chao Chen, Ping Wang
Summary: This study successfully prepared three different morphological and structural phenol-soluble modulin alpha 3 (PSM alpha 3) assemblies using the strategy of salt-inducing assembly polymorphism. It was found that amyloid fibrillation was essential for enhancing the cytotoxicity of PSM alpha 3, and the size and structure of PSM alpha 3 fibrils played a crucial role in cytotoxicity. The cytotoxicity was achieved through a membrane-disrupting mechanism, with different fibril types causing membrane thinning or perforation.
Article
Materials Science, Characterization & Testing
A. Catarina V. D. dos Santos, Bernhard Lendl, Georg Ramer
Summary: A reliable and time-saving protocol for measuring polymers at the nanoscale using photothermal-induced resonance (AFM-IR) was developed and successfully applied to four industrially relevant polymers in this study. The protocol allowed quick analysis and identification of major components of each polymer, including mineral fillers in the blends, without prior knowledge of sample composition.
Article
Chemistry, Physical
Siddhartha Banerjee, Ayanjeet Ghosh
Summary: The aggregation of tau protein plays a central role in neurodegenerative diseases, with the study revealing structural heterogeneities in tau aggregates associated with different diseases, as well as multiple fibrillar polymorphs within the same tau aggregate. Additionally, mature fibrils were found to contain significant amounts of antiparallel beta sheets. The research demonstrates the promise of using nanoscale infrared spectroscopy for spatially resolved investigation of protein aggregation.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2021)
Article
Biochemistry & Molecular Biology
Zeyaul Islam, Mohamed H. Ali, Anton Popelka, Raghvendra Mall, Ehsan Ullah, Janarthanan Ponraj, Prasanna R. Kolatkar
Summary: Amyloid fibrillation, related to various neurological disorders, was studied by examining lysozyme fibrillation using nano-infrared spectroscopy (nanoIR). The study showed that lysozyme transformed into mainly parallel beta-sheets in its fibrillar structure, and nanoIR can complement other biophysical studies in analyzing the aggregation process for potential therapeutic design against amyloid disorders.
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
(2021)
Article
Biochemical Research Methods
Rohini Morey, Alexei Ermolenkov, Wiliam Z. Payne, Douglas C. Scheuring, Jeffrey W. Koym, M. Isabel Vales, Dmitry Kurouski
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
(2020)
Article
Chemistry, Analytical
Lei Zhou, Dmitry Kurouski
ANALYTICAL CHEMISTRY
(2020)
Article
Chemistry, Analytical
Lee Sanchez, David Baltensperger, Dmitry Kurouski
ANALYTICAL CHEMISTRY
(2020)
Article
Chemistry, Physical
Zhandong Li, Dmitry Kurouski
JOURNAL OF PHYSICAL CHEMISTRY C
(2020)
Article
Food Science & Technology
Kyung-Min Lee, Danielle Yarbrough, Mena M. Kozman, Timothy J. Herrman, Jinhyuk Park, Rui Wang, Dmitry Kurouski
FOOD AND CHEMICAL TOXICOLOGY
(2020)
Article
Chemistry, Analytical
Rui Wang, Ian Mangion, Alexey A. Makarov, Dmitry Kurouski
JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS
(2020)
Article
Plant Sciences
Charles Farber, Rebecca Bryan, Li Paetzold, Charles Rush, Dmitry Kurouski
FRONTIERS IN PLANT SCIENCE
(2020)
Article
Plant Sciences
Lee Sanchez, Alexei Ermolenkov, Sudip Biswas, Endang M. Septiningsih, Dmitry Kurouski
FRONTIERS IN PLANT SCIENCE
(2020)
Article
Biochemistry & Molecular Biology
Charles Farber, A. S. M. Faridul Islam, Endang M. Septiningsih, Michael J. Thomson, Dmitry Kurouski
Summary: Digital farming aims to increase crop yield and reduce environmental impact, requiring the development of sensors. This study demonstrates the potential use of Raman spectroscopy for accurately identifying nutrient components in various rice genotypes, providing a new possibility for seed variety identification.
Article
Biochemistry & Molecular Biology
Nicolas K. Goff, James F. Guenther, John K. Roberts, Mickal Adler, Michael Dalle Molle, Greg Mathews, Dmitry Kurouski
Summary: This study explores the potential of Raman spectroscopy (RS) for rapid detection and identification of hermaphroditic cannabis plants. Results show a drastic difference in biochemistry between male, female, and hermaphroditic cannabis plants, allowing for confirmatory identification using a hand-held Raman spectrometer. Machine learning approaches enable accurate identification of hermaphrodites with 98.7% accuracy, while male and female plants can be identified with 100% accuracy.
Article
Biochemistry & Molecular Biology
Mackenzi Peterson, Dmitry Kurouski
Summary: The study investigates the potential of near-infrared Raman spectroscopy (NIRS) in the identification of dyes on fabric. Through the analysis of the vibrational fingerprints of 15 different dyes on cotton, NIRS enables highly accurate identification of dyes, opening up a new avenue for forensic analysis at crime scenes.
Article
Chemistry, Analytical
Alexis Balde, Charles Farber, Mark Krimmer, Daniel Wescott, Dmitry Kurouski
FORENSIC CHEMISTRY
(2020)
Article
Chemistry, Analytical
Fernando Contreras, Alexei Ermolenkov, Dmitry Kurouski
ANALYTICAL METHODS
(2020)
Article
Chemistry, Multidisciplinary
Charles Farber, Lee Sanchez, Dmitry Kurouski
Review
Chemistry, Multidisciplinary
Dmitry Kurouski, Alexandre Dazzi, Renato Zenobi, Andrea Centrone
CHEMICAL SOCIETY REVIEWS
(2020)