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• W2004049075 abstract "We synthesized cyclic disulfide-bonded (i, i + 4) peptides with various net positive charges (+2–+5) from linear peptides derived from the α helical domain of Tenecin 1, an insect defensin, and investigated the effect of the intradisulfide bridge (i, i + 4) on hydrophobicity, secondary structure, leakage activity and binding activity for large unilamellar vesicles, antimicrobial activity, and hemolytic activity. Intradisulfide bridge formation of the peptides resulted in the increase of amphiphilicity and hydrophobicity. Cyclic forms of the peptides did not deeply penetrate into PG/PC (1:1, mole ratio) large unilamellar vesicles and had a decreased lipid membrane perturbation activity for PG/PC LUVs. When the peptides interacted with PG/CL (2:1, mole ratio) LUVs, cyclic peptides with a high net positive charge (+4–+5) showed similar binding affinities and leakage activities for vesicles to those of linear forms, whereas cyclic peptides with a low net positive charge (+2–+3) exhibited lower leakage activity than their linear forms. CD spectra indicate that the intradisulfide bridge (i, i + 4) provided little conformational constraint to linear peptides in buffer solution but resulted in the decrease of α helicity of the peptides in lipid membrane mimic conditions. The cyclic peptide with the highest net positive charge had a similar antibacterial activity to that of the linear peptide, whereas the cyclic peptides with a low net positive charge (+3–+4) exhibited lower antibacterial activity than their linear forms. The cyclic peptides of an appropriate net charge showed more potent activities against some bacteria than those of linear forms under high salt conditions." @default.
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• W2004049075 date "2008-04-01" @default.
• W2004049075 modified "2023-10-17" @default.
• W2004049075 title "Design and synthesis of cyclic disulfide-bonded antibacterial peptides on the basis of the α helical domain of Tenecin 1, an insect defensin" @default.
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• W2004049075 doi "https://doi.org/10.1016/j.bmc.2008.01.019" @default.
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