Improvement of solid material for affinity resins by application of long PEG spacers to capture the whole target complex of FK506

Bioorg Med Chem Lett. 2015 Jul 15;25(14):2788-92. doi: 10.1016/j.bmcl.2015.05.014. Epub 2015 May 15.


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.

Keywords: Affinity resins; Benzenesulfonamide; Calcineurin; Carbonic anhydrase II; FK506; FKBP12; PEG; Target complex; Target identification.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcineurin / chemistry
  • Calcineurin / metabolism
  • Carbonic Anhydrase II / chemistry
  • Carbonic Anhydrase II / metabolism
  • Drug Design
  • Polyethylene Glycols / chemistry*
  • Protein Binding
  • Resins, Synthetic / chemistry*
  • Sulfonamides / chemistry
  • Sulfonamides / metabolism
  • Tacrolimus / chemistry*
  • Tacrolimus / metabolism


  • Resins, Synthetic
  • Sulfonamides
  • Polyethylene Glycols
  • benzenesulfonamide
  • Calcineurin
  • Carbonic Anhydrase II
  • Tacrolimus