A5063441153- Alzheimer's disease research and treatments
- Protein Structure and Dynamics
- Enzyme Structure and Function
- Prion Diseases and Protein Misfolding
- Glycosylation and Glycoproteins Research
- Spectroscopy Techniques in Biomedical and Chemical Research
- Supramolecular Self-Assembly in Materials
- Advanced Glycation End Products research
- Pancreatic function and diabetes
- Bacterial Genetics and Biotechnology
- Proteins in Food Systems
- Protein Interaction Studies and Fluorescence Analysis
- Amyloidosis: Diagnosis, Treatment, Outcomes
- Metabolomics and Mass Spectrometry Studies
- Diet, Metabolism, and Disease
- Orbital Angular Momentum in Optics
- Lipid Membrane Structure and Behavior
- Endoplasmic Reticulum Stress and Disease
- Spectroscopy and Quantum Chemical Studies
- RNA and protein synthesis mechanisms
- Food Industry and Aquatic Biology
- Microfluidic and Bio-sensing Technologies
- Machine Learning in Bioinformatics
- Microtubule and mitosis dynamics
- Nuclear Structure and Function
Kobe University
2014-2024
Osaka University
2004-2012
Protein Research Foundation
2005-2012
Ritsumeikan University
2008-2011
Japan Science and Technology Agency
2005-2009
Centre de Recherche en Économie et Statistique
2006-2007
Centre for Research in Engineering Surface Technology
2006-2007
Centre for Cellular and Molecular Biology
2005
University of Fukui
2005
Kyoto University
2000-2004
Because of the insolubility and polymeric properties amyloid fibrils, techniques used conventionally to analyze protein structure dynamics have often been hampered. Ultrasonication can induce monomeric solution amyloidogenic proteins form fibrils. However, ultrasonication break down preformed fibrils into shorter Here, combining these 2 opposing effects on beta(2)-microglobulin (beta2-m), a responsible for dialysis-related amyloidosis, we present that pulses are useful preparing...
Investigation of factors that modulate amyloid formation proteins is important to understand and mitigate amyloid-related diseases. To the role electrostatic interactions effect ionic cosolutes, especially anions, on formation, we have investigated salts such as NaCl, NaI, NaClO(4), Na(2)SO(4) fibril growth beta(2)-microglobulin, protein involved in dialysis-related amyloidosis. Under acidic conditions, these exhibit characteristic optimal concentrations where favored. The presence leads an...
Abstract The nucleation event of amyloid fibrils is one the most crucial processes that dictate timing and rate pathology diseases; however, information regarding how protein molecules associate to produce fibril nuclei currently limited. In order explore this issue in more detail, we performed time-resolved small angle X-ray scattering (SAXS) measurements on insulin fibrillation, combination with additional multidirectional analyses thioflavin T fluorescence, FTIR spectroscopy, light...
Abstract The thermodynamic hypothesis of protein folding, known as the “Anfinsen’s dogma” states that native structure a represents free energy minimum determined by amino acid sequence. However, inconsistent with Anfinsen’s dogma, globular proteins can misfold to form amyloid fibrils, which are ordered aggregates associated diseases such Alzheimer’s and Parkinson’s diseases. Here, we present general concept for link between folding misfolding. We tested accessibility state various upon...
The formation of amyloid fibrils proceeds via a nucleation-dependent mechanism in which nucleation phase is generally associated with high free energy resulting the rate-limiting step. On basis this kinetic feature, one most crucial phases controlling pathogenesis amyloidoses, but little known about details how protein molecules and surrounding environment vary at stage. Here, we applied near infrared (NIR) spectral monitoring water structural changes real time during fibrillation insulin....
Although the stability of globular proteins has been studied extensively, that amyloid fibrils is scarcely characterized. β 2 ‐microglobulin (β2‐m) a major component observed in patients with dialysis‐related amyloidosis. We effects guanidine hydrochloride on β2‐m, revealing cooperative unfolding transition similar to native state. The increased addition ammonium sulfate, consistent role hydrophobic interactions. results indicate analysis useful obtain insight into structural fibrils.
Beta2-microglobulin (beta2-m) is a major component of amyloid fibrils deposited in patients with dialysis-related amyloidosis. Recent studies have focused on the mechanism by which are formed under physiological conditions, had been difficult to reproduce quantitatively. Yamamoto et al. (Yamamoto, S., Hasegawa, K., Yamaguchi, I., Tsutsumi, Kardos, J., Goto, Y., Gejyo, F. & Naiki, H. (2004) Biochemistry 43, 11075-11082) showed that combination seed prepared acidic conditions and low...
Volume can provide informative structural descriptions of macromolecules such as proteins in solution because a final volumetric outcome accompanies the exquisite equipoise packing effects between residues, and residues waters inside outside proteins. Here we performed systematic investigations on nature amyloidogenic conformations beta2-microglobulin (beta2-m) its core peptide, K3, using high precision densitometer. The transition from acid-denatured beta2-m to mature amyloid fibrils was...
The polymorphic property of amyloid structures has been focused on as a molecular basis the presence and propagation different phenotypes diseases, although little is known about mechanism for expressing diverse from only one protein sequence. Here, we have found that, in combination with an enhancing effect ultrasonication nucleation, β(2)-microglobulin, responsible dialysis-related amyloidosis, generates distinct fibril conformations concentration-dependent manner 2,2,2-trifluoroethanol...
Abstract The replacement of Phe120 with other hydrophobic residues causes a decrease in the activity and thermal stability ribonuclease A (RNase A). To explain this, crystal structures wild‐type RNase three mutants—F120A, F120G, F120W—were analyzed up to 1.4 Å resolution. Although overall backbone all mutant samples were nearly same as that A, except for C‐terminal region F120G high B‐factor, two local conformational changes observed at His119 mutants. First, F120W adopted an position,...
Beta2-microglobulin (beta2-m), a protein responsible for dialysis-related amyloidosis, adopts an immunoglobulin domain fold in its native state. Although beta2-m has Trp residues at positions 60 and 95, both are located near the surface of domain. Hence, does not have conserved common to other domains, which is buried close proximity disulfide bond. To study structure amyloid fibrils relation their fold, we prepared series mutants. Trp60 Trp95 were replaced with Phe, single was introduced...
Elucidating the link between amyloid fibril formation and liquid–liquid phase separation (LLPS) is crucial in understanding pathologies of various intractable human diseases. However, effect condensed protein droplets generated by LLPS on nucleation (the initial step formation) remains unclear because lack available quantitative analysis techniques. This study aimed to develop a measurement method for droplet rate based image analysis. We developed fix micrometer-sized gel long-term...
Non-fibrillar protein aggregates that appear in the earlier stages of amyloid fibril formation are sometimes considered to play a key role nucleation; however, structural features these currently remain unclear. We herein identified characteristic pathway by human insulin B chain, which two major species prefibrillar were identified. Based on time-resolved tracking this with far-UV circular dichroism (CD) spectroscopy, dynamic light scattering (DLS), and 1H-NMR first aggregate hydrodynamic...
Amyloid beta peptide is genetically fused with a ferritin monomer. When the 24-mer cage formed, 24 Aβ peptides are encapsulated and form β-sheet-rich oligomer which can be directly visualized by high-speed AFM after disassembly.
Abstract Optical trapping at interfaces has recently gained relevance due to the expansion of optical potential far away from focus, especially for proteins where submillimeter structures have been described. Initially, lysozyme clusters are trapped as a shallow layer surface, becoming thicker with irradiation time. Nonetheless, overcoming concentration threshold, inside solution collected and transported toward invading layer, which results in border between them, although no jump is...