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Channel formation by polypeptides with a β-helical conformation is known for a head-to-head dimer of a pentadecapeptide gramicidinA;
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Channel formation by polypeptides with a β-helical conformation is known for a head-to-head dimer of a pentadecapeptide gramicidinA;
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Oxidation of the sulfoxide to a sulfone led to changes in the physicochemical properties of the peptides and their mimetics. For examples, see:
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We confirmed that none of the seven analogues tested (2-8) have membrane-disrupting activity at 100nM using liposomes encapsulating carboxyfluorescein (CF).
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We confirmed that none of the seven analogues tested (2-8) have membrane-disrupting activity at 100nM using liposomes encapsulating carboxyfluorescein (CF).
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45
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84874758136
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Charged groups attached to the Cterminus of gramicidinA are known to affect its channel behaviors. For examples, see:
-
Charged groups attached to the Cterminus of gramicidinA are known to affect its channel behaviors. For examples, see:
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