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Long chain amines and long chain ammonium salts as novel inhibitors of dynamin GTPase activity.

Hill, Timothy A (author)
Odell, Luke R (author)
Quan, Annie (author)
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Abagyan, Ruben (author)
Ferguson, Gemma (author)
Robinson, Phillip J (author)
McCluskey, Adam (author)
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Elsevier BV, 2004
2004
English.
In: Bioorganic & Medicinal Chemistry Letters. - : Elsevier BV. - 0960-894X .- 1464-3405. ; 14:12
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • We examined a number of ligands with the view of inhibiting the GTPase activity of dynamin. Dynamin contains a pleckstrin homology (PH) domain that interacts with lipids. We report a series of simple lipid-like molecules that display moderate inhibitory activity. Inhibitory activity is linked to chain length and quaternarization of the terminal amine. A change in the counterion, Cl versus Br or I, had little effect on potency. However, introduction of a hydrophobic collar proximal to the charged site was beneficial to dynamin GTPase inhibitory action. The most potent compound was myristoyl trimethyl ammonium bromide (MTMAB, IC(50) 3.15 microM).

Subject headings

NATURVETENSKAP  -- Kemi -- Organisk kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences -- Organic Chemistry (hsv//eng)

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