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Protein Organic Chemistry Lab
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The lab chemically synthesizes proteins and studies how they work.
AboutAbout the lab
Approaching protein function through chemical synthesis
The Protein Organic Chemistry Lab develops methods for building proteins by chemically linking amino acids, and studies the function of the proteins it makes from the viewpoint of organic chemistry.
With the common method of making proteins by introducing a gene into E. coli, it is not possible to make proteins carrying phosphate groups or glycans, or proteins that are toxic to E. coli.
The lab aims to establish a method that can synthesize any protein, including those embedded in cell membranes and poorly soluble in water, and those carrying modifications.
Taking advantage of the strengths of chemical synthesis to approach protein function, the lab also hopes to advance the design of new proteins and the development of new drugs.
Key terms
- Glycan
- A molecule in which sugars are linked together like a chain. It can attach to proteins, and has been found to play important roles.
- Peptide
- A molecule made of linked amino acids. A long chain of them is a protein.
- Histone
- A protein in the cell nucleus that is responsible for packaging DNA. It also controls gene expression.
NewsLab news
A doctoral student won a poster award at the 19th Chinese International Peptide Symposium
A paper on β2-microglobulin was published
A paper from a collaboration with a former Assistant Professor was published
A review article on the thioester method was published
Collaborative research with the Australian National University was published as a paper
ResearchResearch themes
The lab aims to develop methods for efficiently synthesizing proteins chemically and to study the function of the synthesized proteins from the viewpoint of organic chemistry. It aims to develop a general chemical synthesis method that can also be used for membrane proteins, to study the function of the proteins it synthesizes, and to develop protein-based drugs.
*Illustrative imageSynthesis of glycosylated histone H2A
To study the role of glycosylation of histones, the lab chemically synthesized histone H2A carrying a sugar. By combining glycopeptide synthesis with sequential ligation of four peptides, the protein can now be obtained in large amounts in a short time.
*Illustrative imageSynthesis of glycopeptides containing sialic acid
Sialic acid is sensitive to acid and has been thought to break down easily during peptide synthesis. By using a protecting group that responds to acid, the lab made it possible to produce glycopeptides containing sialic acid with a method no different from conventional peptide synthesis.
*Illustrative imageLinking four peptides with selenoesters
The lab developed a method that uses selenoesters to link four peptide fragments in sequence without a single purification step. Using this method, it synthesized the full length of the enzyme superoxide dismutase.
*Illustrative imageLinking three peptides without purification
By combining CPE and NAC, which are precursors of thioesters, the lab developed a one-pot native chemical ligation (NCL) method that links three peptides without intermediate purification. With this method, it succeeded in chemically synthesizing human histone H4.
MembersFaculty
The members of the Protein Organic Chemistry Lab are faculty, project researchers, doctoral, master's, and undergraduate students, and administrative assistants.As of 2026
- ProfessorHironobu Hojo
- Assistant ProfessorToshiki Takei
- Assistant ProfessorYoshiki Taguchi
- Project ProfessorToshifumi Takao
- Project ProfessorMichio Murata
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Report an errorAbout the images
The top and research theme images are illustrative and were not taken at the lab. They are cropped from Wikimedia Commons images. Cropped CC BY-SA images are provided under the same CC BY-SA license as the original (version shown on each line).
- Top image: “Peptide synthesizer” Michael Pereckas from Milwaukee, WI, USA / CC BY-SA 2.0 (cropped)
- Synthesis of glycosylated histone H2A: “Glycosylation of a polypeptide” Kep17 / CC BY-SA 4.0 (cropped)
- Synthesis of glycopeptides containing sialic acid: “Fluorescense Handful of light” Mateusz Urban / CC BY 4.0 (cropped)
- Linking four peptides with selenoesters: “PDB 1avm EBI” Jawahar Swaminathan and MSD staff at the European Bioinformatics Institute / Public domain (cropped)
- Linking three peptides without purification: “Cryo-EM structure of the human nucleosome Histone H4 8KB5” Hirai S, Kujirai T, Akatsu M, Ogasawara M, Ehara H, Sekine SI, Ohkawa Y, Takizawa Y, Kurumizaka H / CC0 (cropped)
- Related lab (Protein Crystallography Lab (Kurisu Lab)): “SHOC2 Protein Crystal Structure” Achaparro0600 / CC BY-SA 4.0 (cropped)
- Related lab (Supramolecular Structure Analysis Lab): “National Synchrotron Light Source II Quadrupole Magnet Model” Henrysz / CC BY 4.0 (cropped)
- Related lab (Electron Structural Biology Lab): “FEI Titan 50-300 PICO” ER-C, Forschungszentrum Jülich / CC BY-SA 4.0 (cropped)
- Related lab (Functional Structure Measurement Lab): “900 MHz unshielded Oxford magnet Svenskt NMR centrum Gothenburg” Adville / CC BY-SA 4.0 (cropped)
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