本文選題：CC趨化因子受體　切入點(diǎn)：拮抗肽　出處：《中國(guó)病理生理雜志》2015年07期

【摘要】：目的:利用噬菌體展示肽庫(kù)技術(shù)淘選與大鼠CC趨化因子受體5(CCR5)膜外第一、二胞外環(huán)特異性結(jié)合的短肽,并鑒定其與CCR5的結(jié)合能力。方法:在蛋白質(zhì)數(shù)據(jù)庫(kù)中查得大鼠CCR5第一、二胞外環(huán)的氨基酸序列,合成相應(yīng)的線性短肽作為淘選的靶分子,利用噬菌體展示7肽文庫(kù)進(jìn)行3~4輪淘選,用ELISA法鑒定所選肽與靶分子的結(jié)合,并測(cè)定其與濃度的關(guān)系。結(jié)果:與CCR5第一、二胞外環(huán)特異性結(jié)合的噬菌體展示的短肽序列分別為GHWKVWL和HYIDFRW,ELISA鑒定呈陽(yáng)性反應(yīng),且短肽與靶分子的結(jié)合具有濃度依賴性和可飽和性。結(jié)論:利用噬菌體展示技術(shù)成功獲得了2條CCR5特異性結(jié)合的短肽,并在體外證明其可與CCR5第一、二胞外環(huán)具有結(jié)合能力。
[Abstract]:Aim: to elucidate the specific binding of short peptides to rat CC chemokine receptor 5 (CCR5) by phage display peptide library, and to identify the binding ability of the peptide to CCR5.Methods: the amino acid sequences of the first and second extracellular rings of rat CCR5 were identified in the protein database, and the corresponding linear short peptides were synthesized as target molecules for panning. The phage display 7 peptide library was used for 34 rounds of panning.The binding of the selected peptide to the target molecule was identified by ELISA, and the relationship between the peptide and the concentration was determined.Results: the short peptide sequences displayed by phage binding to the first and second extracellular rings of CCR5 were GHWKVWL and HYIDFRWN Elisa, respectively, and the binding of short peptides to target molecules was concentration-dependent and saturable.Conclusion: two short peptides of CCR5 binding were successfully obtained by phage display technique, and it was proved in vitro that they could bind to the first and second extracellular rings of CCR5.
【作者單位】： 中山大學(xué)孫逸仙紀(jì)念醫(yī)院消化內(nèi)科;廣東藥學(xué)院附屬第一醫(yī)院消化內(nèi)科;中山大學(xué)孫逸仙紀(jì)念醫(yī)院兒科;
【基金】：國(guó)家自然科學(xué)資金基助項(xiàng)目(No.81370499) 廣東省自然科學(xué)基金資助項(xiàng)目(No.2014-A030313020)
【分類號(hào)】：R574.62

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本文編號(hào)：1702641