@article { WOS:000284059500031,
	title = {Cyclic peptide inhibitors of HIV-1 integrase derived from the LEDGF/p75 protein},
	journal = {BIOORGANIC \& MEDICINAL CHEMISTRY},
	volume = {18},
	year = {2010},
	month = {DEC 1},
	pages = {8388-8395},
	abstract = {Restricting linear peptides to their bioactive conformation is an attractive way of improving their stability and activity. We used a cyclic peptide library with conformational diversity for selecting an active and stable peptide that mimics the structure and activity of the HIV-1 integrase (IN) binding loop from its cellular cofactor LEDGF/p75 (residues 361-370). All peptides in the library had the same primary sequence, and differed only in their conformation. Library screening revealed that the ring size and linker structure had a huge effect on the conformation, binding and activity of the peptides. One of the cyclic peptides, c(MZ 4-1), was a potent and stable inhibitor of IN activity in vitro and in cells even after 8 days. The NMR structure of c(MZ 4-1) showed that it obtains a bioactive conformation that is similar to the parent site in LEDGF/p75. (C) 2010 Elsevier Ltd. All rights reserved.},
	issn = {0968-0896},
	doi = {10.1016/j.bmc.2010.09.046},
	url = {https://www.sciencedirect.com/science/article/pii/S0968089610008837?via\%3Dihub},
	author = {Hayouka, Zvi and Mattan Hurevich and Levin, Aviad and Benyamini, Hadar and Iosub, Anat and Maes, Michal and Deborah E. Shalev and Loyter, Abraham and Gilon, Chaim and Assaf Friedler}
}
