Abstract
We investigated the structure-antimicrobial activity relationship of tachyplesin I (T-I). Even when Lys1 and Trp2 were both deleted from the N-terminal end of T-I, the antimicrobial activity against gram-negative bacteria was not decreased. But as Lys1 and Trp2 were deleted one by one, the antimicrobial activity against gram-positive bacteria and antiviral activity were gradually decreased. Deletion of two disulfide bridges caused a significant decrease in all activities. The circular dichroism (CD) spectra revealed that the analogs containing the two disulfide bridges took a beta-sheet structure and that the analogs without the disulfide bridges took a random coil conformation. These results suggest that the beta-sheet structure maintained by two disulfide bridges plays an important role in the antimicrobial activity of T-I.
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