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首页> 外文期刊>The Journal of Antibiotics: An International Journal >Identification of Antibiotic Clarithromycin Binding Peptide Displayed by T7 Phage Particles
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Identification of Antibiotic Clarithromycin Binding Peptide Displayed by T7 Phage Particles

机译：T7噬菌体颗粒显示的抗生素克拉霉素结合肽的鉴定

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摘要

Peptide libraries displayed by T7 phage,which contain random cDNA fragments insets,were screened for their ability to bind to a biotinylated derivative of clarithromycin.Phage particles bound to an immobilized derivative of the antibiotic were isolated and the inserted cDNA was amplified and sequenced.A common selected peptide sequence,composed of 19 amino acids,was obtained and a synthetic peptide with this sequence was produced.Surface plasmon resonance experiments showed that the synthetic peptide immobilized on a sensor chip bound to clarithromycin and the dissociation constant was determined to be 2.1X10~(-3)M.The dissociation constants of other macrolide antibiotics,erythromycin,roxithromycin,azithromycin and josamycin were also determined to be 5.4X10~(-3)M,6.2X10~(-5)M,1.1 M and 3.4X10~(-2)M,respectively.These results indicated that T7 phage display method might be useful to determine relatively weak interactions between small molecule drugs and the selected peptides which could represent a possible binding site conserved in binding proteins.
机译：筛选T7噬菌体展示的肽库，其中包含随机插入的cDNA片段，并筛选它们与克拉霉素生物素化衍生物结合的能力。分离与固定化抗生素衍生物结合的噬菌体颗粒，并对插入的cDNA进行扩增和测序。获得了由19个氨基酸组成的共同选择的肽序列，并制备了具有该序列的合成肽。表面等离子体共振实验表明，合成肽固定在与克拉霉素结合的传感器芯片上，解离常数确定为2.1X10 〜（-3）M。其他大环内酯类抗生素红霉素，罗霉素，阿奇霉素和交霉素的解离常数也分别为5.4X10〜（-3）M，6.2X10〜（-5）M，1.1 M和3.4X10这些结果表明，T7噬菌体展示方法可能有助于确定小分子药物与选择的肽之间的较弱相互作用。 d代表结合蛋白中保守的可能的结合位点。

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