180748-30-5Relevant articles and documents
Optimization of pentadentate bispidines as bifunctional chelators for 64Cu positron emission tomography (PET)
Comba, Peter,Hunoldt, Sebastian,Morgen, Michael,Pietzsch, Jens,Stephan, Holger,Wadepohl, Hubert
, p. 8131 - 8143 (2013)
Pentadentate bispidine ligands (3,7-diazabicyclo[3.3.1]nonanes) are optimized for maximum complex stability and facile functionalization with respect to their coupling to biological vector molecules and/or fluorescence markers for PET (positron emission t
DMAP-thiourea catalyst and preparation method thereof, and high-molecular-weight biodegradable polyester and preparation method thereof
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Paragraph 0095-0096; 0099, (2021/07/11)
The invention relates to a DMAP-thiourea catalyst and a preparation method thereof as well as high-molecular-weight biodegradable polyester and a preparation method thereof. The DMAP-thiourea catalyst disclosed by the invention has the characteristic of living polymerization when being used for catalyzing ring opening polymerization of O-carboxyl anhydride monomers (OCAs). According to the DMAP-thiourea catalyst disclosed by the invention, a thiourea group is used as Lewis acid, a monomer is activated through a hydrogen bond, DMAP is used as Lewis alkali and a nucleophilic addition monomer, and ring opening polymerization of an OCAs monomer is commonly catalyzed by utilizing an adjacent synergistic effect. Especially, the increased active species are zwitterions, and no alcohol is needed as an initiator. The polymerization speed is high, the reaction temperature is low, and the obtained polyester is high in molecular weight and narrow in distribution. By adjusting the structure of the catalyst, changing the acidity and alkalinity of the catalyst and the steric hindrance of the catalyst and optimizing parameters such as polymerization temperature, concentration and the like, controllable polymerization of the OCAs monomer is realized, and finally, biodegradable polyester with molecular weight as high as 130,000 is obtained.
Design of coordination interaction of Zn(II) complex with oligo-aspartate peptide to afford a high-affinity tag-probe pair
Fuchida, Hirokazu,Tabata, Shigekazu,Shindo, Naoya,Takashima, Ippei,Leng, Qiao,Hatsuyama, Yuji,Hamachi, Itaru,Ojida, Akio
, p. 784 - 791 (2015/06/25)
A complementary recognition pair consisting of a genetically encodable peptide tag and a small molecular probe isa powerful tool to specifically label and manipulate a protein ofinterest under biological conditions. In this study, we report the redesign of a tag-probe pair comprising an oligo-aspartate peptide tag (such as DDDD) and a binuclear zinc complex. Isothermal-titration calorimetry screening of binding between the series of peptides and zinc complexes revealed that the binding affinity was largely influenced by subtle changes of the ligand structure of the probe. However, the binding was tolerant to differences of the tag peptide sequence. Of those tested, a pair containing a peptide tag (DDAADD) and a binuclear zinc complex possessing 4-chloropyridines (3-2Zn(II)) showed the strongest binding affinity (Ka = 3.88 × 105 M-1), which was about 10-fold larger than the conventional pair of D4-peptide tag (DDDD) and 1-2Zn(II) containing nonsubstituted pyridines (Ka = 3.73 × 104 M-1). The strong binding of this new complementary recognition pair enabled the rapid covalent labeling of a tag-fused maltose binding protein with a fluorescent zinc complex, demonstrating its potential utility in protein analysis.