Synthesis and SAR of Thrombin Inhibitors Incorporating a Novel 4-Amino-Morpholinone Scaffold:  Analysis of X-ray Crystal Structure of Enzyme Inhibitor Complex

2003 ◽  
Vol 46 (19) ◽  
pp. 3985-4001 ◽  
Author(s):  
Jonas W. Nilsson ◽  
Ingemar Kvarnström ◽  
Djordje Musil ◽  
Ingemar Nilsson ◽  
Bertil Samulesson
Keyword(s):  
Crystal Structure ◽  
Enzyme Inhibitor ◽  
Thrombin Inhibitors ◽  
X Ray ◽  
Inhibitor Complex

Inhibition of trypsin by carbobenzyloxylysyl chloromethyl ketone: 13C NMR and x-ray diffraction analyses of the enzyme-inhibitor complex

Tetrahedron ◽  
1986 ◽  
Vol 42 (12) ◽  
pp. 3269-3276 ◽  
Author(s):  
A.I. Scott ◽  
N.E. Mackenzie ◽  
J.P.G. Malthouse ◽  
W.U. Primrose ◽  
P.E. Fagerness ◽  
...  
Keyword(s):  
13C Nmr ◽  
Enzyme Inhibitor ◽  
X Ray Diffraction ◽  
Chloromethyl Ketone ◽  
X Ray ◽  
Inhibitor Complex

Phenolic P2/P3 Core Motif as Thrombin Inhibitors — Design, Synthesis, and X-Ray Co-Crystal Structure.

ChemInform ◽  
2006 ◽  
Vol 37 (19) ◽  
Author(s):  
Stephen Hanessian ◽  
Eric Therrien ◽  
Willem A. L. van Otterlo ◽  
Malken Bayrakdarian ◽  
Ingemar Nilsson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thrombin Inhibitors ◽  
Design Synthesis ◽  
Core Motif ◽  
X Ray

Molecular Modeling of the Aldose Reductase-Inhibitor Complex Based on the X-ray Crystal Structure and Studies with Single-Site-Directed Mutants

2000 ◽  
Vol 43 (6) ◽  
pp. 1062-1070 ◽  
Author(s):  
Suresh B. Singh ◽  
Michael S. Malamas ◽  
Thomas C. Hohman ◽  
Ramaswamy Nilakantan ◽  
Deborah A. Carper ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Molecular Modeling ◽  
Aldose Reductase ◽  
Reductase Inhibitor ◽  
Aldose Reductase Inhibitor ◽  
Single Site ◽  
X Ray ◽  
Inhibitor Complex

Phenolic P2/P3 core motif as thrombin inhibitors—Design, synthesis, and X-ray co-crystal structure

2006 ◽  
Vol 16 (4) ◽  
pp. 1032-1036 ◽  
Author(s):  
Stephen Hanessian ◽  
Eric Therrien ◽  
Willem A.L. van Otterlo ◽  
Malken Bayrakdarian ◽  
Ingemar Nilsson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thrombin Inhibitors ◽  
Design Synthesis ◽  
Core Motif ◽  
X Ray

scholarly journals Structural basis of sialidase in complex with geranylated flavonoids as potent natural inhibitors

2014 ◽  
Vol 70 (5) ◽  
pp. 1357-1365 ◽  
Author(s):  
Youngjin Lee ◽  
Young Bae Ryu ◽  
Hyung-Seop Youn ◽  
Jung Keun Cho ◽  
Young Min Kim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Domain ◽  
Enzyme Inhibitor ◽  
Gastrointestinal Diseases ◽  
Structural Basis ◽  
Cellular Interactions ◽  
Inhibitory Effects ◽  
Inhibitor Complex ◽  
Structural Framework ◽  
Natural Inhibitors

Sialidase catalyzes the removal of a terminal sialic acid from glycoconjugates and plays a pivotal role in nutrition, cellular interactions and pathogenesis mediating various infectious diseases including cholera, influenza and sepsis. An array of antiviral sialidase agents have been developed and are commercially available, such as zanamivir and oseltamivir for treating influenza. However, the development of bacterial sialidase inhibitors has been much less successful. Here, natural polyphenolic geranylated flavonoids which show significant inhibitory effects againstCp-NanI, a sialidase fromClostridium perfringens, are reported. This bacterium causes various gastrointestinal diseases. The crystal structure of theCp-NanI catalytic domain in complex with the best inhibitor, diplacone, is also presented. This structure explains how diplacone generates a stable enzyme–inhibitor complex. These results provide a structural framework for understanding the interaction between sialidase and natural flavonoids, which are promising scaffolds on which to discover new anti-sialidase agents.

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