13798-75-9Relevant articles and documents
SYNTHESIS OF AMINO ACID BONDED SILICA GEL VIA ACTIVE ESTER WITH N-HYDROXYSUCCINIMIDE
Watanabe, Noriyuki
, p. 1331 - 1332 (1981)
The surface of silica gel was chemically modified by amino acid via active ester with N-hydroxysuccinimide.The formations of insoluble by-product and fine particle coming from silica gel, which occur in DCC method were avoided.The amounts of amino acid coupling to silica gel were about twice larger than that by DCC method.
Thermodynamic and Structural Investigation of Synthetic Actinide-Peptide Scaffolds
Safi, Samir,Jeanson, Aurélie,Roques, Jérome,Solari, Pier Lorenzo,Charnay-Pouget, Florence,Den Auwer, Christophe,Creff, Ga?lle,Aitken, David J.,Simoni, Eric
supporting information, p. 877 - 886 (2016/02/03)
The complexation of uranium and europium, in oxidation states +VI and +III, respectively, was investigated with pertinent bio-inorganic systems. Three aspartate-rich pentapeptides with different structural properties were selected for study to rationalize the structure-affinity relationships. Thermodynamic results, crosschecked by both isothermal titration calorimetry and time-resolved laser fluorescence spectroscopy, showed different affinity depending on the peptide for both Eu(III) and U(VI). The thermodynamic aspects were correlated to structural predictions, which were acquired by density functional theory quantum chemical calculations and from IR and extended X-ray absorption fine structure experiments. The combination of these microscopic properties revealed that carbonyl-metal interactions affected the entropy in the case of europium, while the larger uranyl cation was mostly affected by preorganization and steric effects, so that the affinity was enhanced through enthalpy. The approach described here revealed various microscopic aspects governing peptide actinide affinity. Highlighting these mechanisms should certainly contribute to the rational synthesis of higher affinity biomimetic aspartic ligands.
Synthesis and biological evaluation of boron peptide analogues of Belactosin C as proteasome inhibitors
Nakamura, Hiroyuki,Watanabe, Mizuyoshi,Ban, Hyun Seung,Nabeyama, Wataru,Asai, Akira
scheme or table, p. 3220 - 3224 (2010/04/05)
A series of boron peptides 11, 13, 15 and 17 were designed and synthesized as proteasome inhibitors based on the structure of Belactosin C. Matteson homologation was a key step in the synthesis of the boron peptides. Compounds 11a and 13 showed significant inhibition of 20S proteasome chymotrypsin-like (β5) activity (IC50 = 0.28 and 0.51 μM, respectively). Furthermore, like PS-341, compound 11a increased the G2/M cell distribution. A biparametric cytofluorimetric analysis with FITC-labeled annexin V and propidium iodide showed induction of apoptosis by compound 11a at >1 μM concentrations of compound.