A Multistep Approach to Structure-Based Drug Design:  Studying Ligand Binding at the Human Neutrophil Elastase†

2006 ◽  
Vol 49 (6) ◽  
pp. 1837-1844 ◽  
Author(s):  
Thomas Steinbrecher ◽  
David A. Case ◽  
Andreas Labahn
Keyword(s):  
Drug Design ◽  
Ligand Binding ◽  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Human Neutrophil Elastase ◽  
Structure Based Drug Design

Computational methods for calculation of protein-ligand binding affinities in structure-based drug design

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Zbigniew Dutkiewicz
Keyword(s):  
Drug Design ◽  
Ligand Binding ◽  
Binding Free Energy ◽  
Development Project ◽  
Quantum Mechanical ◽  
Prediction Methods ◽  
Binding Affinities ◽  
Structure Based Drug Design ◽  
Quantum Mechanical Description ◽  
Optimization Stage

AbstractDrug design is an expensive and time-consuming process. Any method that allows reducing the time the costs of the drug development project can have great practical value for the pharmaceutical industry. In structure-based drug design, affinity prediction methods are of great importance. The majority of methods used to predict binding free energy in protein-ligand complexes use molecular mechanics methods. However, many limitations of these methods in describing interactions exist. An attempt to go beyond these limits is the application of quantum-mechanical description for all or only part of the analyzed system. However, the extensive use of quantum mechanical (QM) approaches in drug discovery is still a demanding challenge. This chapter briefly reviews selected methods used to calculate protein-ligand binding affinity applied in virtual screening (VS), rescoring of docked poses, and lead optimization stage, including QM methods based on molecular simulations.

scholarly journals Flavonoids as inhibitors of human neutrophil elastase

2021 ◽  
Vol 36 (1) ◽  
pp. 1016-1028
Author(s):  
Katarzyna Jakimiuk ◽  
Jakub Gesek ◽  
Atanas G. Atanasov ◽  
Michał Tomczyk
Keyword(s):  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Human Neutrophil Elastase

Inhibition of Human Neutrophil Elastase with Peptidyl Electrophilic Ketones. 2. Orally Active PG-Val-Pro-Val Pentafluoroethyl Ketones

1994 ◽  
Vol 37 (26) ◽  
pp. 4538-4553 ◽  
Author(s):  
Michael R. Angelastro ◽  
Larry E. Baugh ◽  
Philippe Bey ◽  
Joseph P. Burkhart ◽  
Teng-Man Chen ◽  
...  
Keyword(s):  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Human Neutrophil Elastase ◽  
Orally Active

Optimisation of a human neutrophil elastase assay and investigation of the effect of sesquiterpene lactones

Biologicals ◽  
2005 ◽  
Vol 33 (3) ◽  
pp. 175-184 ◽  
Author(s):  
Karin Schorr ◽  
Anita Rott ◽  
FernandoBatista Da Costa ◽  
Irmgard Merfort
Keyword(s):  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Sesquiterpene Lactones ◽  
Human Neutrophil Elastase

scholarly journals Elastase as a marker for neutrophilic myeloid cells.

1984 ◽  
Vol 32 (4) ◽  
pp. 389-394 ◽  
Author(s):  
J A Kramps ◽  
P van der Valk ◽  
M M van der Sandt ◽  
J Lindeman ◽  
C J Meijer
Keyword(s):  
Cell Lines ◽  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Myeloid Cells ◽  
Hematopoietic Cell ◽  
Human Neutrophil Elastase ◽  
Specific Marker ◽  
Neoplastic Cells ◽  
Myeloproliferative Diseases ◽  
Myelomonocytic Leukemia

The immunohistochemical results obtained with antibodies directed against human neutrophil elastase is described. It was found that neutrophil elastase can be used as a specific marker of cells of the neutrophilic lineage. In normal hematopoietic cell preparations, only promyelocytes and more differentiated myeloid cells stain positive for elastase. In acute or chronic myeloid and myelomonocytic leukemia, the same neutrophil myeloid cells stain positive, whereas neoplastic cells of the monocytoid line are negative. Using elastase in conjunction with other markers, it is possible to differentiate easily the involvement of different cell lines in myeloproliferative diseases.

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