Biomimetic Design of Platelet Adhesion Inhibitors to Block Integrin α2β1-Collagen Interactions: II. Inhibitor Library, Screening, and Experimental Validation

Langmuir ◽  
2014 ◽  
Vol 30 (16) ◽  
pp. 4734-4742 ◽  
Author(s):  
Lin Zhang ◽  
Chao Zhang ◽  
Yan Sun
Keyword(s):  
Experimental Validation ◽  
Platelet Adhesion ◽  
Library Screening ◽  
Biomimetic Design

In Silico Chemical Library Screening and Experimental Validation of a Novel 9-Aminoacridine Based Lead-Inhibitor of Human S-Adenosylmethionine Decarboxylase.

ChemInform ◽  
2007 ◽  
Vol 38 (49) ◽  
Author(s):  
Wesley H. Brooks ◽  
Diane E. McCloskey ◽  
Kenyon G. Daniel ◽  
Steven E. Ealick ◽  
John A. III Secrist ◽  
...  
Keyword(s):  
In Silico ◽  
Experimental Validation ◽  
Library Screening ◽  
Chemical Library ◽  
Adenosylmethionine Decarboxylase

scholarly journals In silico chemical library screening and experimental validation of novel compounds with potential varroacide activities

2019 ◽  
Vol 160 ◽  
pp. 11-19
Author(s):  
Clémence Riva ◽  
Peggy Suzanne ◽  
Gaël Charpentier ◽  
Fabienne Dulin ◽  
Marie-Pierre Halm-Lemeille ◽  
...  
Keyword(s):  
In Silico ◽  
Experimental Validation ◽  
Library Screening ◽  
Chemical Library

Chemical Library Screening Using a SPR-Based Inhibition in Solution Assay: Simulations and Experimental Validation

2013 ◽  
Vol 85 (18) ◽  
pp. 8787-8795 ◽  
Author(s):  
Laurence Choulier ◽  
Yves Nominé ◽  
Gabrielle Zeder-Lutz ◽  
Sebastian Charbonnier ◽  
Bruno Didier ◽  
...  
Keyword(s):  
Experimental Validation ◽  
Library Screening ◽  
Chemical Library

In Silico Chemical Library Screening and Experimental Validation of a Novel 9-Aminoacridine Based Lead-Inhibitor of Human S-Adenosylmethionine Decarboxylase

2007 ◽  
Vol 47 (5) ◽  
pp. 1897-1905 ◽  
Author(s):  
Wesley H. Brooks ◽  
Diane E. McCloskey ◽  
Kenyon G. Daniel ◽  
Steven E. Ealick ◽  
John A. Secrist ◽  
...  
Keyword(s):  
In Silico ◽  
Experimental Validation ◽  
Library Screening ◽  
Chemical Library ◽  
Adenosylmethionine Decarboxylase

Fine Structure of Platelet Interaction with a New Microcrystalline Collagen Preparation

1974 ◽  
Vol 32 ◽  
pp. 58-59
Author(s):  
W. H. Zucker ◽  
R. G. Mason
Keyword(s):  
Fine Structure ◽  
Platelet Aggregation ◽  
Hydrochloric Acid ◽  
Whole Blood ◽  
Platelet Adhesion ◽  
Hemostatic Agent ◽  
Native Collagen ◽  
Fibrillar Morphology ◽  
Clinical Interest ◽  
New Form

Platelet adhesion initiates platelet aggregation and is an important component of the hemostatic process. Since the development of a new form of collagen as a topical hemostatic agent is of both basic and clinical interest, an ultrastructural and hematologic study of the interaction of platelets with the microcrystalline collagen preparation was undertaken.In this study, whole blood anticoagulated with EDTA was used in order to inhibit aggregation and permit study of platelet adhesion to collagen as an isolated event. The microcrystalline collagen was prepared from bovine dermal corium; milling was with sharp blades. The preparation consists of partial hydrochloric acid amine collagen salts and retains much of the fibrillar morphology of native collagen.

Experimental validation of the predicted TGR5 binding mode model

2015 ◽  
Vol 53 (01) ◽  
Author(s):  
L Spomer ◽  
CGW Gertzen ◽  
D Häussinger ◽  
H Gohlke ◽  
V Keitel
Keyword(s):  
Experimental Validation ◽  
Binding Mode

Von Willebrand disease and Weibel-Palade bodies

2010 ◽  
Vol 30 (03) ◽  
pp. 150-155 ◽  
Author(s):  
J. W. Wang ◽  
J. Eikenboom
Keyword(s):  
Platelet Adhesion ◽  
Coagulation Factor ◽  
Von Willebrand Disease ◽  
Inflammatory Factors ◽  
Limited Data ◽  
Storage Organelle ◽  
And Function ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryVon Willebrand factor (VWF) is a pivotal haemostatic protein mediating platelet adhesion to injured endothelium and carrying coagulation factor VIII (FVIII) in the circulation to protect it from premature clearance. Apart from the roles in haemostasis, VWF drives the formation of the endothelial cell specific Weibel-Palade bodies (WPBs), which serve as a regulated storage of VWF and other thrombotic and inflammatory factors. Defects in VWF could lead to the bleeding disorder von Willebrand disease (VWD).Extensive studies have shown that several mutations identified in VWD patients cause an intracellular retention of VWF. However, the effects of such mutations on the formation and function of its storage organelle are largely unknown. This review gives an overview on the role of VWF in WPB biogenesis and summarizes the limited data on the WPBs formed by VWD-causing mutant VWF.

Inhibition of Platelet Adhesion to Fibrin(ogen) in Flowing Whole Blood by Arg-Gly-Asp and Fibrinogen γ-Chain Carboxy Terminal Peptides

1992 ◽  
Vol 68 (06) ◽  
pp. 694-700 ◽  
Author(s):  
Roy R Hantgan ◽  
Silvia C Endenburg ◽  
I Cavero ◽  
Gérard Marguerie ◽  
André Uzan ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Whole Blood ◽  
Platelet Adhesion ◽  
Integrin Receptor ◽  
Shear Rates ◽  
Perfusion Chamber ◽  
Receptor Recognition ◽  
Adhesive Interactions ◽  
Coated Surfaces ◽  
Carboxy Terminal

SummaryWe have employed synthetic peptides with sequences corresponding to the integrin receptor-recognition regions of fibrinogen as inhibitors of platelet aggregation and adhesion to fibrinogen-and fibrin-coated surfaces in flowing whole blood, using a rectangular perfusion chamber at wall shear rates of 300 s–1 and 1,300 s–1. D-RGDW caused substantial inhibition of platelet aggregation and adhesion to fibrinogen and fibrin at both shear rates, although it was least effective at blocking platelet adhesion to fibrin at 300 s–1. RGDS was a weaker inhibitor, and produced a biphasic dose-response curve; SDRG was inactive. HHLGGAK-QAGDV partially inhibited platelet aggregation and adhesion to fibrin(ogen) at both shear rates. These results support the identification of an RGD-specific receptor, most likely the platelet integrin glycoprotein IIb: III a, as the primary receptor responsible for platelet: fibrin(ogen) adhesive interactions under flow conditions, and indicate that platelet adhesion to surface bound fibrin(ogen) is stabilized by multivalent receptor-ligand contacts.

Platelet Adhesion to Native Collagens Involves Proteoglycans and May Be a Two-Step Process

1987 ◽  
Vol 58 (02) ◽  
pp. 786-789 ◽  
Author(s):  
O Behnke
Keyword(s):  
Electron Microscope ◽  
Platelet Adhesion ◽  
Close Contact ◽  
Blood Platelets ◽  
Collagen Fibrils ◽  
Platelet Membrane ◽  
Step Process ◽  
Rat Blood ◽  
Wide Gap ◽  
Rat Tail

SummaryAdhesion of rat blood platelets to native rat tail collagen fibrils was studied in the electron microscope under conditions that preserved collagen-associated proteoglycans (CAPG). The CAPG molecules were aligned in chain-like configurations that encircled the fibrils with a 65 nm period; they appeared to coat the fibrils completely and extended 60-100 nm away from the fibril. The initial platelet-fibril contact occurred between the platelet glycocalyx and the CAPG of the fibrils i.e. between two surfaces with net-negative charges. When close contact was established between the fibril surface proper and the platelet membrane, CAPG were not identified in the area of contact, and the collagen-platelet distance was reduced to a ~10-12 nm wide gap traversed by delicate links in register with fibril periodicities.

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