1099718-55-4Relevant academic research and scientific papers
Enzyme promotes the hydrogelation from a hydrophobic small molecule
Gao, Jie,Wang, Huaimin,Wang, Ling,Wang, Jingyu,Kong, Deling,Yang, Zhimou
supporting information; experimental part, p. 11286 - 11287 (2011/03/19)
(Chemical Equation Presented) We report in this paper that an enzymatic reaction can be used as the sole mechanism for forming supramolecular hydrogels that have good stability in aqueous solutions at room temperature. The gels are two-component hydrogels that are mainly formed by hydrophobic compound 2 and doped with hydrophilic compound 1. They were formed by an enzymatic process that produces hydrophobic 2 in homogeneous modes and assists the formation of three-dimensional networks. We have characterized the morphologies of the gels with scanning electron microscopy and dark-field transmission electron microscopy, collected fluorescence data to monitor the gelation process, and proposed a possible mechanism to explain the formation of the gels.
A phosphotyrosine-imprinted polymer receptor for the recognition of tyrosine phosphorylated peptides
Emgenbroich, Marco,Borrelli, Cristiana,Shinde, Sudhirkumar,Lazraq, Issam,Vilela, Filipe,Hall, Andrew J.,Oxelbark, Joakim,De Lorenzi, Ersilia,Courtois, Julien,Simanova, Anna,Verhage, Jeroen,Irgum, Knut,Karim, Kai,Sellergren, Boerje
experimental part, p. 9516 - 9529 (2009/11/30)
Hyperphosphorylation at tyrosine is commonly observed in tumor proteomes and, hence, specific phosphoproteins or phosphopeptides could serve as markers useful for cancer diagnostics and therapeutics. The analysis of such targets is, however, a challenging
