133565-45-4Relevant articles and documents
Modified Nucleobases with Uniform H-Bonding Interactions, Homo- and Hetero-Basepair Bias, and Mismatch Discrimination
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Paragraph 0014, (2021/07/30)
Described herein are divalent nucleobases that each binds two nucleic acid strands, matched or mismatched when incorporated into a nucleic acid or nucleic acid analog backbone, such as in a γ-peptide nucleic acid (γPNA). Also provided are genetic recognition reagents comprising one or more of the divalent nucleobases and a nucleic acid or nucleic acid analog backbone, such as a γPNA backbone. Uses for the divalent nucleobases and monomers and genetic recognition reagents containing the divalent nucleobases also are provided.
Straightforward Entry to S -Glycosylated Fmoc-Amino Acids and Their Application to Solid Phase Synthesis of Glycopeptides and Glycopeptidomimetics
Comegna, Daniela,De Paola, Ivan,Saviano, Michele,Del Gatto, Annarita,Zaccaro, Laura
, p. 640 - 643 (2015/03/05)
Streamlined access to S-glycosylated Fmoc-amino acids was developed. The process provides diverse glycosylated modified amino acids in high yield and stereoselectivity taking advantage of the in situ generation of a glycosylthiolate obtained from carbohyd
A peptide aldehyde microarray for high-throughput profiling of cellular events
Wu, Hao,Ge, Jingyan,Yang, Peng-Yu,Wang, Jigang,Uttamchandani, Mahesh,Yao, Shao Q.
, p. 1946 - 1954 (2011/04/16)
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 P1-P4 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.
