38585-73-8Relevant articles and documents
Amine modification of digested peptide at C-terminal end during protein digestion by protease
Ito, Toshiyuki,Sugita, Yoshiaki,Takao, Koichi,Ikeguchi, Yoshihiko,Shirahata, Akira
, p. 1838 - 1843 (2007)
We recently reported that C-terminal polyamine modification occurs when proteins are digested with trypsin in the presence of polyamine [Biochem. Biophys. Res. Commun., 356, 159-162 (2007)]. In the present study, the characteristics of this C-terminal modification in the presence of protease and amine were investigated. When hemoglobin (HB) was digested with trypsin in the presence of N-(2-pyridyl)-1,4-diaminobutane (Py4), formation of the modified peptide was dependent on time and on HB or Py4 concentration. When synthetic peptide was treated with trypsin in the presence of Py4, ca. 0.1% of the peptide was modified with Py4. When HB or cytochrome C was treated with a range of serine proteases in the presence of various amines (Py4, N-(2-pyridyl)-1,3- diaminopropane, tranexamic acid, isonicotinic acid hydrazide and ampicillin), the modified peptide was detected in all cases tested, thus suggesting that amine modification widely accompanies digestion by proteases.
N-{3-[(1,1-dioxido-1,2-benzothiazol-3-yl)(phenyl)amino]propyl}benzamide analogs as potent Kv1.3 inhibitors. Part 1
Haffner, Curt D.,Thomson, Stephen A.,Guo, Yu,Schaller, Lee T.,Boggs, Sharon,Dickerson, Scott,Gobel, Jeff,Gillie, Dan,Condreay, J. Patrick
scheme or table, p. 6983 - 6988 (2010/12/25)
We report the synthesis and in vitro activity of a series of novel N-{3-[(1,1-dioxido-1,2-benzothiazol-3-yl)(phenyl)amino]propyl}benzamide analogs. These analogs showed potent inhibitory activity against Kv1.3. Several compounds, including compound 8b, sh
Integrin receptors antagonists
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Page/Page column 79, (2010/11/23)
The invention relates to novel compounds which bind to integrin receptors, and to the preparation thereof and the use thereof as drugs.