Blar i forfatter "Sugiyama, Satoshi"

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    • Design of galardine analogs as putative psudolysin inhibitors based on ab initio fragment molecular orbital calculations 

      Ezawa, Takuya; Sugiyama, Satoshi; Ara, Ayami; Sylte, Ingebrigt; Kurita, Noriyuki (Journal article; Tidsskriftartikkel; Peer reviewed, 2019-08-29)
      Pseudolysin (PLN) is a metalloproteinase secreted from bacteria that degrades extracellular proteins to produce bacterial nutrition. It is thus expected that inhibitors against PLN can suppress the growth of bacteria and their pandemic spread. In addition, since these inhibitors do not attack to bacteria directly, there is a reduced risk for producing drug-resistant bacteria. On the other hand, as ...

    • Proposal of selective inhibitor for bacterial zinc metalloprotease: Molecular mechanics and ab initio molecular orbital calculations 

      Imai, Kyohei; Saito, Rysouke; Ezawa, Takyua; Sugiyama, Satoshi; Sylte, Ingebrigt; Kurita, Noriyuki (Journal article; Tidsskriftartikkel; Peer reviewed, 2022-10-11)
      The zinc metalloprotease pseudolysin (PLN) secreted from Pseudomonas aeruginosa degrades extracellular proteins to produce bacterial nutrition, and various types of PLN inhibitors have been developed to suppress the bacterial growth. However, as the structure of the ligand-binding pocket of PLN has large similarities to those of human matrix metalloproteinases (MMPs) and other human zinc metalloprotease, ...

    • Protonation states of central amino acids in a zinc metalloprotease complexed with inhibitor: Molecular mechanics optimizations and ab initio molecular orbital calculations 

      Ezawa, Takuya; Saito, Ryosuke; Suzuki, Shusuke; Sugiyama, Satoshi; Sylte, Ingebrigt; Kurita, Noriyuki (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-04-01)
      The zinc-metalloprotease pseudolysin (PLN) secreted from bacteria degrades extracellular proteins to produce bacterial nutrition. Since PLN has a Zn ion at the inhibitor-binding site, the interactions between Zn and PLN residues as well as inhibitor can be significantly changed depending on the protonation states of PLN residues at the inhibitor-binding site. To determine stable protonation states ...