New light on the "old" chloride channel blocker DIDS

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

4,4′-Diisothiocyanatostilbene-2,2′-disulfonic acid (DIDS) has been used as an inhibitor of anion transporters and channels since the early 1970s. A study in this issue shows that DIDS hydrolyzes in aqueous solution and then multimerizes to di-, tri-, tetra-, and pentameric polythioureas, which inhibit both the bacterial ClC-ec1 Cl-/H+ exchanger and the mammalian ClC-Ka chloride channel 3-200 times more potently than DIDS itself. The DIDS tetra- and pentamer could potentially act as tethered blockers that simultaneously obstruct both chloride pathways in the dimeric CLC proteins.

Original languageEnglish (US)
Pages (from-to)399-401
Number of pages3
JournalACS Chemical Biology
Volume3
Issue number7
DOIs
StatePublished - Jul 18 2008

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Chloride Channels
Light
Acids
Anions
Chlorides
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

Cite this

New light on the "old" chloride channel blocker DIDS. / Wulff, Heike.

In: ACS Chemical Biology, Vol. 3, No. 7, 18.07.2008, p. 399-401.

Research output: Contribution to journalArticle

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