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71.
Offermann DA McKendrick JE Sejberg JJ Mo B Holdom MD Helm BA Leatherbarrow RJ Beavil AJ Sutton BJ Spivey AC 《The Journal of organic chemistry》2012,77(7):3197-3214
The disruption of the human immunolobulin E-high affinity receptor I (IgE-FcεRI) protein-protein interaction (PPI) is a validated strategy for the development of anti asthma therapeutics. Here, we describe the synthesis of an array of conformationally constrained cyclic peptides based on an epitope of the A-B loop within the Cε3 domain of IgE. The peptides contain various tolan (i.e., 1,2-biarylethyne) amino acids and their fully and partially hydrogenated congeners as conformational constraints. Modest antagonist activity (IC(50) ~660 μM) is displayed by the peptide containing a 2,2'-tolan, which is the one predicted by molecular modeling to best mimic the conformation of the native A-B loop epitope in IgE. 相似文献
72.
Fanzhi Kong Goreti Ribeiro Morais Robert A. Falconer Chris W. Sutton 《Tetrahedron letters》2012,53(5):546-549
Phosphatidylcholine analogues were synthesised as affinity ligands for the capture of membrane proteins. Several protecting group strategies were investigated to synthesize the amino-functionalized phosphatidylcholine: 11-aminoundecyl 2-(trimethylammonio)ethyl phosphate (4). The acid-mediated deprotection of the Boc group generated a mixture of the target products which could only be purified by HPLC. However, an alternative strategy, using the hydrazine-labile phthalimide group route, followed by a gel filtration step proved straightforward to afford the desired amino-functionalized phosphatidylcholine product in high yield and purity. 相似文献
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74.
Lee Chiachunq Peters Walter H. Sutton Michael A. Chao Yuh J. 《Experimental Techniques》1985,9(6):26-27
Experimental Techniques - 相似文献
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Summary Os2(CO)8Cl2
(1) is orthorhombic P212121 witha=9.3599(9),b=9.879(2),c=16.014(3), V=14803, Dc=3.03 Mgm–3 for Z=4. Structure solved by Patterson methods. Final R=0.038, Rw=0.038 [w=(2F)] for 1270 observed reflections and 141 parameters. Os3(CO)12Cl2
(2) is monoclinic C2/m witha=12.105(3), b=10.612(3),c=8.798(1) , =117.02(2)°, V=10063, Dc=3.22 Mgm–3 for Z=2. Structure solved by Patterson methods. Final R=0.036, Rw=0.037 (w=(2F)–) for 821 observed reflections and 75 parameters.Complex(1) has an osmium-osmium single bond 2.897(1), with the chloride ligands in equatorial positions,(2) has a linear triosmium chain with osmium-osmium single bonds 2.893(1) and the chloride ligands occupy equatorial sites on the terminal osmium atoms. Both(1) and(2) are isostructural with their osmium carbonyl iodide analogues. 相似文献
79.
Csorna SE Mestayer MD Panvini RS Word GB Yi X Bean A Bobbink GJ Brock I Engler A Ferguson T Kraemer R Rippich C Sutton R Vogel H Bebek C Berkelman K Blucher E Cassel DG Copie T DeSalvo R DeWire JW Ehrlich R Galik RS Gilchriese MG Gittelman B Gray SW Halling AM Hartill DL Heltsley BK Holzner S Ito M Kandaswamy J Kowalewski R Kreinick DL Kubota Y Mistry NB Mueller J Nordberg E Ogg M Peterson D Perticone D Pisharody M Read K Riley D Silverman A Stein PC Stone S Sadoff AJ Avery P Besson D Bowcock T 《Physical review letters》1986,56(12):1222-1225
80.
Low-molecular-weight human serum proteome using ultrafiltration, isoelectric focusing, and mass spectrometry 总被引:1,自引:0,他引:1
Identification of the serum proteome is a daunting analytical task due to the complex nature of the sample which has an extremely large dynamic range of protein components. This report addresses this issue by using centrifugal ultrafiltration to enrich the low-molecular-weight (LMW) serum proteome while decreasing the amount of abundant high-molecular-weight proteins. Reduction of the complex nature of the sample was achieved by fractionation of the LMW serum proteins using solution-phase isoelectric focusing (IEF). Multiple enzyme digestions are performed and analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Analysis of the tandem mass spectra resulted in the identification of 262 proteins belonging to LMW serum proteome. Our results demonstrate the effectiveness of this methodology to isolate and identify LMW proteins with improved confidence in the MS data acquired. In addition, our methodology can be combined with other multidimensional chromatography techniques performed on the peptide level to increase the number of identified proteins. 相似文献