Stapled peptides with improved potency and specificity that activate p53

Please use this identifier to cite or link to this item: https://doi.org/10.1021/cb3005148

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. https://doi.org/10.1021/cb3005148
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
URI:	http://scholarbank.nus.edu.sg/handle/10635/101720
ISSN:	15548929
DOI:	10.1021/cb3005148
Appears in Collections:	Staff Publications

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