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IsCT is a non-cell-selective antimicrobial peptide isolated from the scorpion Opisthacanthus madagascariensis that has potent cytolytic activity against both mammalian and bacterial cells. To investigate the structure-activity relationships of IsCT and to design novel peptide antibiotics with bacterial cell selectivity, we synthesized several analogs of(More)
Indolicidin (IN) is a 13-residue Trp-rich antimicrobial peptide isolated from bovine neutrophils. To develop novel IN-derived antimicrobial peptides with enhanced cell specificity (therapeutic index) and potent anti-inflammatory activity, several IN analogs were synthesized by Pro-->Lys substitution. All IN analogs displayed an increase in therapeutic index(More)
Ib-AMP1 is a 20-residue disulfide-linked beta-sheet antimicrobial peptide found in the seeds of Impatiens balsamina. In order to investigate the effects of the 2 disulfide bonds on the antimicrobial specificity, to determine the mechanism of antimicrobial action of Ib-AMP1 and to develop novel cell-selective antimicrobial peptides with improved(More)
Here, we report the successful design of a novel bacteria-selective antimicrobial peptide, Pep-1-K (KKTWWKTWWTKWSQPKKKRKV). Pep-1-K was designed by replacing Glu-2, Glu-6, and Glu-11 in the cell-penetrating peptide Pep-1 with Lys. Pep-1-K showed strong antibacterial activity against reference strains (MIC = 1-2 microM) of Gram-positive and Gram-negative(More)
The cell-penetrating peptide Tat (48-60) (GRKKRRQRRRPPQ) derived from HIV-1 Tat protein showed potent antibacterial activity (MIC: 2-8 microM). To investigate the effect of dimerization of Tat (48-60) analog, [Tat(W): GRKKRRQRRRPWQ-NH(2)], on antimicrobial activity and mechanism of bactericidal action, its dimeric peptides, di-Tat(W)-C and di-Tat(W)-K, were(More)
VSTx1 is a voltage sensor toxin from the spider Grammostola spatulata that inhibits KvAP, an archeabacterial voltage-activated K(+) channel whose X-ray structure has been reported. Although the receptor for VSTx1 and the mechanism of inhibition are unknown, the sequence of the toxin is related to hanatoxin (HaTx) and SGTx, two toxins that inhibit eukaryotic(More)
To develop a useful method for designing cell-selective antimicrobial peptides and to investigate the effect of incorporating peptoid residues into an alpha-helical model peptide on structure, function, and mode of action, we synthesized a series of model peptides incorporating Nala (Ala-peptoid) into different positions of an amphipathic alpha-helical(More)
The cell penetrating peptide, penetratin (RQIKIWFQNRRMKWKK-NH2) showed potent antimicrobial activity (MIC: 0.5-4 microM) without any cytotoxicity against mammalian cells. This study investigated the effect of linking together two peptide chains of penetratin on antimicrobial and cytolytic activities and plausible mode of bactericidal action. Two-stranded(More)
HP (2-20), a 19-residue peptide derived from the N-terminus of Helicobacter pylori ribosomal protein L1, has antimicrobial activity but is not cytotoxic to human erythrocytes. We synthesized several peptide analogues to investigate the effects of substitutions on structure and antimicrobial activity. Replacement of Gln16 and Asp18 with tryptophan [anal-3(More)
In antimicrobial peptides, the cationic property due to basic amino acids has been widely recognized as an important factor to promote electrostatic interaction with negatively charged phospholipids. However, little is known about the differences between two basic residues, Arg and Lys, in membrane binding affinity. Tritrpticin is an Arg- or Trp-rich(More)