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Title: Stapled peptides with improved potency and specificity that activate p53
Authors: Brown, C.J.
Quah, S.T.
Jong, J.
Goh, A.M.
Chiam, P.C.
Khoo, K.H.
Choong, M.L.
Lee, M.A.
Yurlova, L.
Zolghadr, K.
Joseph, T.L.
Verma, C.S. 
Lane, D.P.
Issue Date: 15-Mar-2013
Citation: Brown, C.J., Quah, S.T., Jong, J., Goh, A.M., Chiam, P.C., Khoo, K.H., Choong, M.L., Lee, M.A., Yurlova, L., Zolghadr, K., Joseph, T.L., Verma, C.S., Lane, D.P. (2013-03-15). Stapled peptides with improved potency and specificity that activate p53. ACS Chemical Biology 8 (3) : 506-512. ScholarBank@NUS Repository.
Abstract: By using a phage display derived peptide as an initial template, compounds have been developed that are highly specific against Mdm2/Mdm4. These compounds exhibit greater potency in p53 activation and protein-protein interaction assays than a compound derived from the p53 wild-type sequence. Unlike Nutlin, a small molecule inhibitor of Mdm2/Mdm4, the phage derived compounds can arrest cells resistant to p53 induced apoptosis over a wide concentration range without cellular toxicity, suggesting they are highly suitable for cyclotherapy. © 2012 American Chemical Society.
Source Title: ACS Chemical Biology
ISSN: 15548929
DOI: 10.1021/cb3005148
Appears in Collections:Staff Publications

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