Small-molecule peptides inhibit Z α1-antitrypsin polymerization
Version of Record online: 16 DEC 2008
© 2008 The Authors Journal compilation © 2009 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd
Journal of Cellular and Molecular Medicine
Volume 13, Issue 8b, pages 2304–2316, August 2009
How to Cite
Chang, Y.-P., Mahadeva, R., Chang, W.-S. W., Lin, S.-C. and Chu, Y.-H. (2009), Small-molecule peptides inhibit Z α1-antitrypsin polymerization. Journal of Cellular and Molecular Medicine, 13: 2304–2316. doi: 10.1111/j.1582-4934.2008.00608.x
- Issue online: 26 NOV 2009
- Version of Record online: 16 DEC 2008
- Received: June 11, 2008; Accepted: October 27, 2008
Fig. S1 Iterative deconvolution of the first two rounds of libraries binding to M-AT. The library screening was performed with the 8 M urea PAGE and potency of sub-libraries was judged by the formation of binary complex (BC). (A) and (B) show the first and second round of screening, respectively. The initial screening condition was performed with a calculated 100-fold molar excess of each individual peptide of AT. Incubations were performed at 37°C for 2 hrs, and then given with a heat-pulse of 20 min. at 62°C before gel electrophoresis. The letters below each graph are standard amino acid symbols.
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