161403-90-3Relevant articles and documents
NOVEL CARBONATE ANALOGUES BEARING PTEROSTILBENE AMINO ACIDS FOR THE TREATMENT OF NON-ALCOHOLIC FATTY LIVER DISEASE AND NON-ALCOHOLIC STEATOHEPATITIS
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Page/Page column 40-41, (2021/12/31)
A series of novel analogs of water soluble pterostilbene amino acid bearing carbonates were synthesized, which show activities in treating a non-alcoholic fatty liver disease and a nonalcoholic steatohepatitis (NASH).
Comparison of alternative nucleophiles for Sortase A-mediated bioconjugation and application in neuronal cell labelling
Baer, Samuel,Nigro, Julie,Madej, Mariusz P.,Nisbet, Rebecca M.,Suryadinata, Randy,Coia, Gregory,Hong, Lisa P. T.,Adams, Timothy E.,Williams, Charlotte C.,Nuttall, Stewart D.
, p. 2675 - 2685 (2014/05/06)
The Sortase A (SrtA) enzyme from Staphylococcus aureus catalyses covalent attachment of protein substrates to pentaglycine cross-bridges in the Gram positive bacterial cell wall. In vitro SrtA-mediated protein ligation is now an important protein engineering tool for conjugation of substrates containing the LPXTGX peptide recognition sequence to oligo-glycine nucleophiles. In order to explore the use of alternative nucleophiles in this system, five different rhodamine-labelled compounds, with N-terminal nucleophilic amino acids, triglycine, glycine, and lysine, or N-terminal non-amino acid nucleophiles ethylenediamine and cadaverine, were synthesized. These compounds were tested for their relative abilities to function as nucleophiles in SrtA-mediated bioconjugation reactions. N-Terminal triglycine, glycine and ethylenediamine were all efficient in labelling a range of LPETGG containing recombinant antibody and scaffold proteins and peptides, while reduced activity was observed for the other nucleophiles across the range of proteins and peptides studied. Expansion of the range of available nucleophiles which can be utilised in SrtA-mediated bioconjugation expands the range of potential applications for this technology. As a demonstration of the utility of this system, SrtA coupling was used to conjugate the triglycine rhodamine-labelled nucleophile to the C-terminus of an Im7 scaffold protein displaying Aβ, a neurologically important peptide implicated in Alzheimer's disease. Purified, labelled protein showed Aβ-specific targeting to mammalian neuronal cells. Demonstration of targeting neuronal cells with a chimeric protein illustrates the power of this system, and suggests that SrtA-mediated direct cell-surface labelling and visualisation is an achievable goal. This journal is the Partner Organisations 2014.
Photoresponsive soft nanotubes for controlled guest release
Kameta, Naohiro,Tanaka, Asuka,Akiyama, Haruhisa,Minamikawa, Hiroyuki,Masuda, Mitsutoshi,Shimizu, Toshimi
supporting information; scheme or table, p. 5251 - 5255 (2011/07/07)
Light, transformation, release! Self-assembly of a simple amphiphile with an azobenzene unit produced an organic nanotube with 20 nm inner diameter. The trans-to-cis photoisomerization of the azobenzene unit within the solid bilayer membranes of the nanot
SYNTHESIS AND BIOLOGICAL ACTIVITIES OF NEW ANALOGUES OF β-CASOMORPHINE-5*
Sobirov, M.M.,Khalikov, Sh.Kh.,Saidov, S.S.,Kodirov, M.Z.,Zaitsev, S.V.,et al.
, p. 397 - 405 (2007/10/02)
Four new analogues of β-casomorphine-5 modified at the C-end by modifiers based on ethylenediamine and glycine residues have been synthesized. the opioid and analgesic activities of the peptides obtained comparison with β-casomorphine-5 and morphine are discussed.
