KOBE Chemical Genetics. Inc.

Chūō-ku, Japan

KOBE Chemical Genetics. Inc.

Chūō-ku, Japan
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Mabuchi M.,Health Science University | Mabuchi M.,KOBE Chemical Genetics. Inc. | Shimizu T.,Health Science University | Ueda M.,Health Science University | And 4 more authors.
Bioorganic and Medicinal Chemistry Letters | Year: 2015

Solid materials for affinity resins bearing long PEG spacers between a functional group used for immobilization of a bio-active compound and the solid surface were synthesized to capture not only small target proteins but also large and/or complex target proteins. Solid materials with PEG1000 or PEG2000 as spacers, which bear a benzenesulfonamide derivative, exhibited excellent selectivity between the specific binding protein carbonic anhydrase type II (CAII) and non-specific ones. These materials also exhibited efficacy in capturing a particular target at a maximal amount. Affinity resins using solid materials with PEG1000 or PEG2000 spacers, bear a FK506 derivative, successfully captured the whole target complex of specific binding proteins at the silver staining level, while all previously known affinity resins with solid materials failed to achieve this objective. These novel affinity resins captured other specific binding proteins such as dynamin and neurocalcin δ as well. © 2015 Elsevier Ltd.All rights reserved.


Mabuchi M.,Health Science University | Mabuchi M.,KOBE Chemical Genetics. Inc. | Shimizu T.,Health Science University | Haramura M.,Chugai Pharmaceutical Co. | And 2 more authors.
Bioorganic and Medicinal Chemistry Letters | Year: 2015

Abstract This Letter presents an effective method for the identification of target proteins of bioactive compounds such as drugs, natural products, and intrinsic ligands, using an affinity resin. The application of a photo-labile linker to an affinity resin enabled the selective elution of a target protein by irradiation for a short duration at 4°C while leaving a large amount of non-specific binding protein on the resin. We have named this method the 'STEAP' method (selective target elution from affinity resins with photo-labile linker). Only a target protein that can bind the bioactive compound, the so-called 'active' protein, is eluted by the selective cleavage of the linker between the solid matrix and the target compound, and therefore, it is worth considering the potential of this method for the hyper-purification of proteins. © 2015 Elsevier Ltd.

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