Kentaro Shiraki

ORCID: 0000-0003-3438-4076
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About
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Research Areas
  • Protein purification and stability
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Proteins in Food Systems
  • Monoclonal and Polyclonal Antibodies Research
  • RNA Research and Splicing
  • Viral Infectious Diseases and Gene Expression in Insects
  • Analytical Chemistry and Chromatography
  • Enzyme Catalysis and Immobilization
  • Enzyme Production and Characterization
  • Transgenic Plants and Applications
  • Spectroscopy and Quantum Chemical Studies
  • Protein Interaction Studies and Fluorescence Analysis
  • RNA Interference and Gene Delivery
  • DNA and Nucleic Acid Chemistry
  • Crystallization and Solubility Studies
  • Carbon Nanotubes in Composites
  • Terahertz technology and applications
  • Lipid Membrane Structure and Behavior
  • Glycosylation and Glycoproteins Research
  • Prion Diseases and Protein Misfolding
  • RNA and protein synthesis mechanisms
  • Mass Spectrometry Techniques and Applications
  • Mechanical and Optical Resonators
  • Muscle metabolism and nutrition

University of Tsukuba
2016-2025

University of Cyprus
2023

Alliance Protein Laboratories (United States)
2010-2011

Japan Science and Technology Agency
2010

Tokyo Gakugei University
2010

Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA)
2009

Japan Advanced Institute of Science and Technology
2001-2008

Kitasato University
2008

Osaka University
1995-2005

Protein Research Foundation
1995-2002

Plasma medicine is an attractive new research area, but the principles of plasma modification biomolecules in aqueous solution remain elusive. In this study, we investigated chemical effects atmospheric-pressure cold on 20 naturally occurring amino acids solution. High-resolution mass spectrometry revealed that modifications 14 were observed after treatment: (i) hydroxylation and nitration aromatic rings tyrosine, phenylalanine tryptophan; (ii) sulfonation disulfide linkage formation thiol...

10.1088/0022-3727/47/28/285403 article EN Journal of Physics D Applied Physics 2014-06-24

Each protein folds into a unique and native structure spontaneously. However, during the unfolding or refolding process, often tends to form aggregates. To establish method prevent undesirable aggregation increase stability of structures under deterioration conditions, two types thermal unfolding-induced dilution-induced from denatured state, were studied in presence additional amino acids ions using lysozyme as model protein. Among 15 tested, arginine exhibited best results preventing...

10.1093/oxfordjournals.jbchem.a003261 article EN The Journal of Biochemistry 2002-10-01

Abstract Plasma medicine is an attractive new research area, but fundamental information related to plasma modification of biomacromolecules in aqueous solution remains elusive. As described herein, we investigated the chemical effects low‐temperature atmospheric pressure on protein using lysozyme as a model. treatment decreased enzymatic activity and changed secondary structure that results from increased molecular weight with modification. These arise neither UV light nor heat, suggesting...

10.1002/ppap.201100063 article EN Plasma Processes and Polymers 2011-10-17

Unacceptably high viscosity is observed in protein concentration formulations due to extremely large therapeutic dose of antibodies and volume restriction subcutaneous route administration. Here, we show that a aggregation suppressor, arginine hydrochloride (ArgHCl), specifically decreases antibody formulations. The viscosities bovine gamma globulin (BGG) solution at 250 mg/mL human (HGG) 292 physiological pH were too for injections, but decreased an acceptable level (below 50 cP) the...

10.1021/mp5000218 article EN Molecular Pharmaceutics 2014-04-01

Liquid droplets formed inside the cell by liquid-liquid phase separation maintain membrane-less condensates/bodies (or compartments). These are important for concentrating certain molecules and facilitating spatiotemporal regulation of cellular functions. 1,6-hexanediol (1,6-HD), an aliphatic alcohol, inhibits weak hydrophobic protein-protein/protein-RNA interactions required droplet formation (droplet melting activity) is used here to elucidate process cytoplasmic/nuclear...

10.26508/lsa.202001005 article EN cc-by Life Science Alliance 2021-02-03

Proteins tend to form inactive aggregates at high temperatures. We show that polyamines, which have a relatively simple structure as oligoamids, effectively prevent thermal inactivation and aggregation of hen egg lysozyme. In the presence additives, including arginine guanidine (100 microM), more than 30% 0.2 mg x mL(-1) lysozyme in sodium phosphate buffer (pH 6.5) formed insoluble by heat treatment (98 degrees C for 30 min). However, 50 mm spermine or spermidine, no were observed after same...

10.1046/j.1432-1033.2003.03850.x article EN European Journal of Biochemistry 2003-10-19

10.1016/j.ijbiomac.2011.11.005 article EN International Journal of Biological Macromolecules 2011-11-19

Liquid–liquid phase separation (LLPS) of proteins and DNA has recently emerged as a possible mechanism underlying the dynamic organization chromatin. We herein report role quadruplex folding in liquid droplet formation via LLPS induced by interactions between linker histone H1 (H1), key regulator chromatin organization. Fluidity measurements inside droplets, binding assays using G-quadruplex-selective probes, structural analyses based on circular dichroism demonstrated that structures, such...

10.1021/jacs.1c03447 article EN Journal of the American Chemical Society 2021-06-21

The poor aqueous solubility of drug substances hampers their broader applications. This paper describes a de novo strategy to increase the using an arginine-assisted solubilization system (AASS) with alkyl gallates as model substances. Solubility experiments showed that arginine greatly increases different gallates, whose solubilities differ widely. In contrast, lysine marginal effects on solubility. Molecular dynamic simulation indicated greater interaction than lysine, which reflects...

10.1021/jp101909a article EN The Journal of Physical Chemistry B 2010-10-06

Several general mechanisms of metallocenter biosynthesis have been reported and reviewed, in all cases, the components or subunits an apoprotein remain final holoprotein. Here, we first discovered that one subunit apoenzyme did not functional holoenzyme. The cobalt-containing low-molecular-mass nitrile hydratase (L-NHase) Rhodococcus rhodochrous J1 consists beta- alpha-subunits encoded by nhlBA genes, respectively. An ORF, nhlE, just downstream nhlBA, was found to be necessary for L-NHase...

10.1073/pnas.0803428105 article EN Proceedings of the National Academy of Sciences 2008-09-23

While biotechnological applications of arginine (Arg) as a solution additive that prevents protein aggregation are increasing, the molecular mechanism its effects remains unclear. In this study, we investigated Arg–lysozyme complex by high-resolution crystallographic analysis. Three Arg molecules were observed to be in close proximity aromatic amino acid residues surface, and their occupancies gradually increased with increasing concentration. These interactions mediated electrostatic,...

10.1093/protein/gzq101 article EN Protein Engineering Design and Selection 2010-11-17

10.1016/j.foodhyd.2017.01.014 article EN Food Hydrocolloids 2017-01-11

Sterilization of certain infected areas the human body surface is necessary for dental and surgical therapies. Because blood filled with fluid, sterilization in solution essential. In vitro has been successively carried out using a combination low-temperature atmospheric-pressure plasma reduced pH method, where sufficiently acidic. Here, we show molecular mechanism such based on microbiology. Three kinds bacteria were inactivated by treatment under various conditions. The theoretical...

10.1088/0022-3727/46/29/295402 article EN Journal of Physics D Applied Physics 2013-07-01

Arginine is a versatile additive to prevent protein aggregation. This paper shows that arginine ethylester (ArgEE) prevents heat‐induced inactivation and aggregation of hen egg lysozyme more effectively than or guanidine. The addition ArgEE decreased the melting temperature lysozyme. data could be interpreted in terms binding unfolded lysozyme, possibly through ethylated carboxyl group, which leads effective prevention intermolecular interaction among aggregation‐prone molecules. suggest...

10.1111/j.1432-1033.2004.04257.x article EN European Journal of Biochemistry 2004-07-14

Proteins have evolved to acquire highly specialized biological functions and are ideal for various applications in both medicine biotechnology, although denaturation is one of the major problems protein chemistry. Here, we show a novel strategy regulation preservation enzymatic activity even after heat treatment by complex formation with cationic smart copolymer, poly(N,N-diethylaminoethyl methacrylate)-graft-poly(ethylene glycol) (PEAMA-g-PEG). PEAMA-g-PEG suppressed lysozyme completely...

10.1021/ja900786z article EN Journal of the American Chemical Society 2009-04-20

Artificial enzyme activators are of great interest for applications in a wide range research fields. Here, we report an hyperactivation system using polyelectrolytes that complementary to charged substrates. The activity α-chymotrypsin (ChT) cationic substrate increased 7-fold at pH 7.0 the presence anionic poly(acrylic acid) (PAAc) and 18-fold poly(allylamine) (PAA). Analysis salt effects, kinetics, dynamic light scattering (DLS), circular dichroism (CD) indicated activation results from...

10.1021/la500575c article EN Langmuir 2014-03-17
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