Title |
Dual-acting stapled peptides target both HIV-1 entry and assembly
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Published in |
Retrovirology, November 2013
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DOI | 10.1186/1742-4690-10-136 |
Pubmed ID | |
Authors |
Hongtao Zhang, Francesca Curreli, Abdul A Waheed, Peter Y Mercredi, Mansi Mehta, Pallavi Bhargava, Daniel Scacalossi, Xiaohe Tong, Shawn Lee, Alan Cooper, Michael F Summers, Eric O Freed, Asim K Debnath |
Abstract |
Previously, we reported the conversion of the 12-mer linear and cell-impermeable peptide CAI to a cell-penetrating peptide NYAD-1 by using an i,i + 4 hydrocarbon stapling technique and confirmed its binding to the C-terminal domain (CTD) of the HIV-1 capsid (CA) protein with an improved affinity (K(d) ~ 1 μM) compared to CAI (K(d) ~ 15 μM). NYAD-1 disrupts the formation of both immature- and mature-like virus particles in in vitro and cell-based assembly assays. In addition, it displays potent anti-HIV-1 activity in cell culture against a range of laboratory-adapted and primary HIV-1 isolates. |
X Demographics
Geographical breakdown
Country | Count | As % |
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United Kingdom | 1 | 50% |
Unknown | 1 | 50% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 2 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Canada | 1 | 2% |
Unknown | 45 | 98% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 10 | 22% |
Researcher | 6 | 13% |
Student > Doctoral Student | 5 | 11% |
Professor | 4 | 9% |
Other | 3 | 7% |
Other | 11 | 24% |
Unknown | 7 | 15% |
Readers by discipline | Count | As % |
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Chemistry | 15 | 33% |
Biochemistry, Genetics and Molecular Biology | 9 | 20% |
Agricultural and Biological Sciences | 7 | 15% |
Medicine and Dentistry | 3 | 7% |
Pharmacology, Toxicology and Pharmaceutical Science | 2 | 4% |
Other | 4 | 9% |
Unknown | 6 | 13% |