Please use this identifier to cite or link to this item:
|Title:||A peptide aldehyde microarray for high-throughput profiling of cellular events||Authors:||Wu, H.
|Issue Date:||16-Feb-2011||Citation:||Wu, H., Ge, J., Yang, P.-Y., Wang, J., Uttamchandani, M., Yao, S.Q. (2011-02-16). A peptide aldehyde microarray for high-throughput profiling of cellular events. Journal of the American Chemical Society 133 (6) : 1946-1954. ScholarBank@NUS Repository. https://doi.org/10.1021/ja109597v||Abstract:||Microarrays provide exciting opportunities in the field of large-scale proteomics. With the aim to elucidate enzymatic activity and profiles within native biological samples, we developed a microarray comprising a focused positional-scanning library of enzyme inhibitors. The library was diversified across P 1-P 4 positions, creating 270 different inhibitor sublibraries which were immobilized onto avidin slides. The peptide aldehyde-based small-molecule microarray (SMM) specifically targeted cysteine proteases, thereby enabling large-scale functional assessment of this subgroup of proteases, within fluorescently labeled samples, including pure proteins, cellular lysates, and infected samples. The arrays were shown to elicit binding fingerprints consistent with those of model proteins, specifically caspases and purified cysteine proteases from parasites (rhodesein and cruzain). When tested against lysates from apoptotic Hela and red blood cells infected with Plasmodium falciparum, clear signatures were obtained that were readily attributable to the activity of constituent proteases within these samples. Characteristic binding profiles were further able to distinguish various stages of the parasite infection in erythrocyte lysates. By converting one of our brightest microarray hits into a probe, putative protein markers were identified and pulled down from within apoptotic Hela lysates, demonstrating the potential of target validation and discovery. Taken together, these results demonstrate the utility of targeted SMMs in dissecting cellular biology in complex proteomic samples. © 2011 American Chemical Society.||Source Title:||Journal of the American Chemical Society||URI:||http://scholarbank.nus.edu.sg/handle/10635/92988||ISSN:||00027863||DOI:||10.1021/ja109597v|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Dec 5, 2019
WEB OF SCIENCETM
checked on Dec 5, 2019
checked on Nov 30, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.