A novel peptide shows excellent anti-HIV-1 potency as a gp41 fusion inhibitor |
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Authors: | Wei Liu Xiaohong An Jiao Wang Xiaoguang Zhang Jianjun Tan Zhixiang Zhou Yi Zeng |
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Institution: | 1. College of Life Science and Bioengineering, Beijing University of Technology, Beijing 100124, China;2. State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Centre for Disease Control and Prevention, Beijing 100052, China |
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Abstract: | Fusion inhibitors of HIV prevent the virus from entering into the target cell via the interaction with gp41, which stops the process of spatial rearrangement of the viral envelope protein. A series of peptides have been designed and screened to obtain a highly potent novel sequence. Among them, CT105 possesses the most potent anti-viral ability at low nanomolar IC50 values against a panel of HIV-1 pseudoviruses from A, B, C and A1/D subtypes, whereas T20 shows much weaker potency. CT105 also shows excellent inhibitory activity at 260 pico molar IC50 against HIV-1 replication. As a fusion inhibitor, CT105 has a strong ability to interrupt gp41 core formation. The terminal half-life of CT105 possesses 1.72-fold longer than that of T20 as determined by developing an indirect competitive ELISA method. The results suggest that this artificial peptide CT105 could be a favorable architype for further optimization and modification. |
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Keywords: | HIV-1 Peptide fusion inhibitor Gp41 ELISA Terminal half-life |
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