Synthesis of analogs of peptides from Buthus martensii scorpion venom with potential antibiotic activity
Synthesis of analogs of peptides from Buthus martensii scorpion venom with potential antibiotic activity
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DOI：
10.1016/j.peptides.2014.10.008
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发表时间：
2015-06-01
期刊：
影响因子：
3
通讯作者：
de Johnson, Laura Elena Luque
中科院分区：
文献类型：
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作者：
Bea, Roberto de la Salud;Ascuitto, Michael Ross;de Johnson, Laura Elena Luque
已合成并测试了在 Buthus martensii Karsh 蝎毒中发现的天然肽 (BmKn1) 的五种类似物，以将其抗菌和溶血活性与野生型进行比较。圆二色光谱显示这些肽形成α螺旋结构，其氨基酸位置预示着两亲性。结果表明，通过用丙氨酸、缬氨酸和亮氨酸连续取代序列的位置 5 和 9（位于螺旋的疏水侧）来增加疏水性，可增强抗菌活性和溶血作用。当通过添加赖氨酸引入更多正电荷来对位置 7 和 10（亲水侧）进行改变时，两种活性也会增加。然而，当引入负电荷（使用谷氨酸）时，观察到抗菌活性，但在研究的浓度下溶血减少至零。虽然强抑制活性在低浓度（10 μg/mL）时开始，但一些肽会消除抑制作用，并且随着浓度的增加没有观察到任何变化。 (C) 2014 Elsevier Inc. 保留所有权利。
Five analogs of a natural peptide (BmKn1) found in the venom of scorpion Buthus martensii Karsh have been synthesized and tested to compare their antimicrobial and hemolytic activity with the wild type. Circular dichroism spectra show that these peptides form an alpha helix structure and its amino acid positions predict an amphipathic nature. Results show that increasing hydrophobicity by substituting successively positions 5 and 9 of the sequence (on the hydrophobic side of the helix) with alanine, valine and leucine enhances antimicrobial activity and hemolysis. When changes are done on positions 7 and 10 (on the hydrophilic side) by introducing more positive charges with addition of lysine, both activities also increase. However, when negative charges are introduced instead (with glutamic acids), antimicrobial activity is observed but hemolysis is reduced to zero under the concentrations studied. Although strong inhibitory activity begins at low concentrations (10 mu g/mL), some peptides level off inhibition and no change is observed as concentrations are increased. (C) 2014 Elsevier Inc. All rights reserved.