906734-92-7Relevant academic research and scientific papers
Light Regulation of Enzyme Allostery through Photo-responsive Unnatural Amino Acids
Kneuttinger, Andrea C.,Straub, Kristina,Bittner, Philipp,Simeth, Nadja A.,Bruckmann, Astrid,Busch, Florian,Rajendran, Chitra,Hupfeld, Enrico,Wysocki, Vicki H.,Horinek, Dominik,K?nig, Burkhard,Merkl, Rainer,Sterner, Reinhard
, p. 1501 - 9,1514 (2019)
Imidazole glycerol phosphate synthase (ImGPS) is an allosteric bienzyme complex in which substrate binding to the synthase subunit HisF stimulates the glutaminase subunit HisH. To control this stimulation with light, we have incorporated the photo-respons
Photoresponsive self-healing supramolecular hydrogels for light-induced release of DNA and doxorubicin
Pianowski, Zbigniew L.,Karcher, Johannes,Schneider, Knut
, p. 3143 - 3146 (2016)
An azobenzene-containing cyclic dipeptide PAP-DKP-Lys is a photoresponsive low-MW hydrogelator. The gelation process can be triggered with temperature, pH, light, and ionic strength. The resulting self-healing gels can encapsulate dsDNA or an anticancer d
Modulating the Phe-Phe dipeptide aggregation landscape via covalent attachment of an azobenzene photoswitch
Johny, Melby,Vijayalakshmi, Kanchustambham,Das, Ankita,Roy, Palas,Mishra, Aseem,Dasgupta, Jyotishman
, p. 9348 - 9351 (2017)
Synthetic control of peptide-based supramolecular assemblies can provide molecular cues to understand protein aggregation while also inspiring the development of novel chemical biology tools to deliver cargoes inside cells. Here we show that the trans-to-
Azobenzene-containing photoswitchable proteasome inhibitors with selective activity and cellular toxicity
Blanco, Beatriz,Palasis, Kathryn A.,Adwal, Alaknanda,Callen, David F.,Abell, Andrew D.
supporting information, p. 5050 - 5054 (2017/09/27)
A series of azobenzene-containing peptidic boronate esters was prepared and the activity of the thermally adapted states (TAS), enriched in trans isomer, and the photostationary states (PSS), enriched in cis isomer, for each compound were evaluated agains
The incorporation of a photoisomerizable amino acid into proteins in E. coli
Bose, Mohua,Groff, Dan,Xie, Jianming,Brustad, Eric,Schultz, Peter G.
, p. 388 - 389 (2007/10/03)
An orthogonal aminoacyl tRNA synthetase/tRNA pair has been evolved that allows the incorporation of the photoisomerizable amino acid phenylalanine-4′-azobenzene (AzoPhe) into proteins in E. coli in response to the amber nonsense codon. Further, we show th
