1352039-29-2Relevant academic research and scientific papers
Probing protease activity by single-fluorescent-protein nanocapsules
Gu, Zhen,Biswas, Anuradha,Joo, Kye-Il,Hu, Biliang,Wang, Pin,Tang, Yi
, p. 6467 - 6469 (2010)
We describe a FRET-based protease detection strategy, using a single-fluorescent-protein nanogel as donor and a dark quencher as acceptor linked by a photolabile caged-peptide. This design enables probing of protease activity in a UV-responsive fashion.
Peptide release upon photoconversion of 2-nitrobenzyl compounds into nitroso derivatives
Nakayama, Koji,Heise, Inge,Goerner, Helmut,Gaertner, Wolfgang
experimental part, p. 1031 - 1035 (2012/08/27)
The photoinduced conversion via the aci-nitro into the nitroso form was studied for 4,5-dimethoxy-2-nitrobenzyl alcohols attached to various leaving groups: amino acids histidine (NHis) and aspartate (NAsp) as well as their fluorenylmethoxycarbonyl derivatives (FHis) and (FAsp). In addition, two peptides containing either of the two amino acids were studied, carrying the photoreactive group attached to a histidine (PHis), or to an aspartate (PAsp). The aci-nitro forms with maximum at λaci = 420 nm were observed for FHis and FAsp after the decay of a triplet-triplet absorption, analogous to those of other 2-nitrobenzyl type compounds. For both FHis and FAsp the quantum yield of photoconversion δ∥p is 0.03 and for the peptides PHis and PAsp ca 0.01 and 0.005, respectively. Photocaged amino acids, histidine and aspartate were incorporated by chemical synthesis into peptides. The peptides show sequence motifs of proteins from the bacterial two-component signaling system. The light-labile protection group, 2-nitro-4,5-dimethoxybenzyl, could be removed by ultraviolet irradiation, releasing the active peptides. In both cases, the triplet forms and the aci-nitro species were generated transiently and yielded the 2-nitroso-4,5-dimethoxybenzaldehyde.
