Practical and Scalable Manufacturing Process for Plasma Kallikrein Inhibitor ASP5069

2020 ◽  
Vol 24 (12) ◽  
pp. 2830-2839
Author(s):  
Shun Hirasawa ◽  
Yoshinori Kohmura
Keyword(s):  
Manufacturing Process ◽  
Plasma Kallikrein ◽  
Kallikrein Inhibitor

P051 QLS-215 IS A LONG-ACTING MONOCLONAL ANTIBODY PLASMA KALLIKREIN INHIBITOR FOR THE POTENTIAL TREATMENT OF HAE

2021 ◽  
Vol 127 (5) ◽  
pp. S28
Author(s):  
P. Bista ◽  
A. Nichols ◽  
T. Kiselak ◽  
P. Harwin ◽  
J. Violin ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Plasma Kallikrein ◽  
Potential Treatment ◽  
Kallikrein Inhibitor ◽  
Long Acting

Berotralstat (BCX7353): Structure-Guided Design of a Potent, Selective, and Oral Plasma Kallikrein Inhibitor to Prevent Attacks of Hereditary Angioedema (HAE)

2021 ◽  
Vol 64 (17) ◽  
pp. 12453-12468
Author(s):  
Pravin L Kotian ◽  
Minwan Wu ◽  
Satish Vadlakonda ◽  
Venkat Chintareddy ◽  
Pengcheng Lu ◽  
...  
Keyword(s):  
Hereditary Angioedema ◽  
Plasma Kallikrein ◽  
Kallikrein Inhibitor

HAE-Prophylaxe mit Plasma-Kallikrein-Inhibitor

2018 ◽  
Vol 27 (6) ◽  
pp. 12-12
Author(s):  
Marie Fahrenhold
Keyword(s):  
Plasma Kallikrein ◽  
Kallikrein Inhibitor

Analysis of an engineered plasma kallikrein inhibitor and its effect on contact activation

2010 ◽  
Vol 391 (4) ◽  
Author(s):  
A. Allart Stoop ◽  
Ravi V. Joshi ◽  
Christopher T. Eggers ◽  
Charles S. Craik
Keyword(s):  
Serine Protease ◽  
Protein Interactions ◽  
Phage Library ◽  
Plasma Kallikrein ◽  
Amino Acid Residues ◽  
Protein Protein Interactions ◽  
Contact Activation ◽  
Kallikrein Inhibitor ◽  
Membrane Type ◽  
Opposing Effects

AbstractEngineering of protein-protein interactions is used to enhance the affinity or specificity of proteins, such as antibodies or protease inhibitors, for their targets. However, fully diversifying all residues in a protein-protein interface is often unfeasible. Therefore, we limited our phage library for the serine protease inhibitor ecotin by restricting it to only tetranomial diversity and then targeted all 20 amino acid residues involved in protein recognition. This resulted in a high-affinity and highly specific plasma kallikrein inhibitor, ecotin-Pkal. To validate this approach we dissected the energetic contributions of each wild type (wt) or mutated surface loop to the binding of either plasma kallikrein (PKal) or membrane-type serine protease 1. The analysis demonstrated that a mutation in one loop has opposing effects depending on the sequence of surrounding loops. This finding stresses the cooperative nature of loop-loop interactions and justifies targeting multiple loops with a limited diversity. In contrast to ecotin wt, the specific loop combination of ecotin-Pkal discriminates the subtle structural differences between the active enzymes, PKal and Factor XIIa, and their respective zymogen forms. We used ecotin-Pkal to specifically inhibit contact activation of human plasma at the level mediated by plasma kallikrein.

scholarly journals Phase 1 Dose-Escalation Study of Plasma Kallikrein Inhibitor THR-149 for the Treatment of Diabetic Macular Edema

2021 ◽  
Vol 10 (14) ◽  
pp. 28
Author(s):  
Pravin U. Dugel ◽  
Arshad M. Khanani ◽  
Brian B. Berger ◽  
Sunil Patel ◽  
Mitchell Fineman ◽  
...  
Keyword(s):  
Macular Edema ◽  
Diabetic Macular Edema ◽  
Dose Escalation ◽  
Phase 1 ◽  
Plasma Kallikrein ◽  
Dose Escalation Study ◽  
Kallikrein Inhibitor

Net Changes in Plasma Kallikrein Inhibitor Levels by Procedure Type and Use of Aprotinin

2002 ◽  
Vol 96 (Sup 2) ◽  
pp. A123
Author(s):  
Elliott Bennett-Guerrero ◽  
Robert J. Frumento ◽  
Ian J. Mackie ◽  
Michael J. Gallimore ◽  
Catherine M.N. OʼMalley
Keyword(s):  
Plasma Kallikrein ◽  
Kallikrein Inhibitor ◽  
Procedure Type
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