English page
Overview of Research
Proteins are biological “machines.” Proteins must “fold” to carry out these functions as machines. However, the process of protein folding remains unclear in many ways. We study the mechanisms of protein folding and the structures of proteins. Our goal is to be able to design the three-dimensional structure of protein.
Research Theme:
Studies on proteins by using NMR method and protein engineering
Research Keywords:
Protein Science, Structural Biology, Protein Engineering, NMR, Innate Immunity, Antimicrobial peptide, Cytokine, NMR metabolomics
Recent Publications:
- The subtype of Cupressaceae pollinosis associated with Pru p 7 sensitization is characterized by a sensitization to a cross-reactive gibberellin-regulated protein in cypress pollen: BP14.
Poncet P, Aizawa T, Sénéchal H.
Clin Exp Allergy, 49, 1163-1166 (2019) - A new allergen family involved in pollen food associated syndrome: snakin/gibberellin regulated proteins.
Sénéchal H, Šantrůček J, Melčová M, Svoboda P, Zídková J, Charpin D, Guilloux L, Shahali Y, Selva MA, Couderc R, Aizawa T, Poncet P.
J Allergy Clin Immunol, 141, 411-414 (2018) - R-Spondin1 expands Paneth cells and prevents dysbiosis induced by graft-versus-host disease.
Hayase E, Hashimoto D, Nakamura K, Noizat C, Ogasawara R, Takahashi S, Ohigashi H, Yokoi Y, Sugimoto R, Matsuoka S, Ara T, Yokoyama E, Yamakawa T, Ebata K, Kondo T, Hiramine R, Aizawa T, Ogura Y, Hayashi T, Mori H, Kurokawa K, Tomizuka K, Ayabe T, Teshima T.
J Exp Med, 214, 3507-3518 (2017) - Enhanced expression of cysteine-rich antimicrobial peptide snakin-1 in Escherichia coli using an aggregation-prone protein coexpression system.
Kuddus MR, Yamano M, Rumi F, Kikukawa T, Demura M, Aizawa T.
Biotechnol Prog, 33, 1520-8 (2017) - Overexpression of Antimicrobial, Anticancer, and Transmembrane Peptides in Escherichia coli through a Calmodulin-Peptide Fusion System.
Ishida H, Nguyen LT, Gopal R, Aizawa T, Vogel HJ.
J Am Chem Soc, 138, 11318-26 (2016) - Lipopolysaccharide-bound structure of the antimicrobial peptide cecropin P1 determined by nuclear magnetic resonance spectroscopy
M. Baek, M. Kamiya, T. Kushibiki, T. Nakazumi, S. Tomisawa, C. Abe, Y. Kumaki, T. Kikukawa, M. Demura, K. Kawano, Keiichi, T. Aizawa
Journal of Peptide Science, , 22, 214-21 (2016) - In vivo fluorescence-correlation spectroscopy analyses of FMBP-1, a silkworm transcription factor
M. Tsutsumi, H.Muto, S. Myoba, M. Kimoto, A. Kitamura, M. Kamiya, T. Kikukawa, S. Takiya, M. Demura, K. Kawano, M. Kinjo, T. Aizawa
FEBS Open Bio, , 6, 106-25 (2016) - Efficient production of a correctly folded mouse a-defensin, cryptdin-4, by refolding during inclusion body solubilization
S. Tomisawa, Y. Sato, M. Kamiya, Y. Kumaki, T. Kikukawa, K. Kawano, M. Demura, K. Nakamura, T. Ayabe, T. Aizawa
Protein Expression and Purification, 112, 21-28 (2015).
Contact:
Tomoyasu AIZAWA, Ph. D.
Professor
Faculty of Advanced Life Science
Hokkaido University
N10, W8, Kita-ku, Sapporo, 060-0810, JAPAN
e:mail: 
