Development of a mono‐specific anti‐VEGF bivalent nanobody with extended plasma half‐life for treatment of pathologic neovascularization

2019 ◽  
Vol 12 (1) ◽  
pp. 92-100 ◽  
Author(s):  
Amir Sadeghi ◽  
Mahdi Behdani ◽  
Serge Muyldermans ◽  
Mahdi Habibi‐Anbouhi ◽  
Fatemeh Kazemi‐Lomedasht
Keyword(s):  
Half Life ◽  
Anti Vegf ◽  
Extended Plasma ◽  
Plasma Half Life ◽  
Pathologic Neovascularization

scholarly journals PASylation of Murine Leptin Leads to Extended Plasma Half-Life and Enhancedin VivoEfficacy

2015 ◽  
Vol 12 (5) ◽  
pp. 1431-1442 ◽  
Author(s):  
Volker Morath ◽  
Florian Bolze ◽  
Martin Schlapschy ◽  
Sarah Schneider ◽  
Ferdinand Sedlmayer ◽  
...  
Keyword(s):  
Half Life ◽  
Extended Plasma ◽  
Plasma Half Life

Benefits and limitations of extended plasma half-life factor VIII products in hemophilia A

2020 ◽  
Vol 29 (3) ◽  
pp. 303-309 ◽  
Author(s):  
Pier Mannuccio Mannucci
Keyword(s):  
Factor Viii ◽  
Half Life ◽  
Hemophilia A ◽  
Extended Plasma ◽  
Plasma Half Life ◽  
Life Factor

Acetylcholinesterase-Fc Fusion Protein (AChE-Fc): A Novel Potential Organophosphate Bioscavenger with Extended Plasma Half-Life

2015 ◽  
Vol 26 (8) ◽  
pp. 1753-1758 ◽  
Author(s):  
Tal Noy-Porat ◽  
Ofer Cohen ◽  
Sharon Ehrlich ◽  
Eyal Epstein ◽  
Ron Alcalay ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Half Life ◽  
Extended Plasma ◽  
Fc Fusion Protein ◽  
Plasma Half Life

Recombinant Fc-Elabela fusion protein has extended plasma half-life andmitigates post-infarct heart dysfunction in rats

2019 ◽  
Vol 292 ◽  
pp. 180-187 ◽  
Author(s):  
Yue Xi ◽  
Daozhan Yu ◽  
Rongze Yang ◽  
Qingbin Zhao ◽  
Junhong Wang ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Half Life ◽  
Heart Dysfunction ◽  
Extended Plasma ◽  
Plasma Half Life

scholarly journals Extended plasma half-life of albumin-binding domain fused human IgA upon pH-dependent albumin engagement of human FcRn in vitro and in vivo

mAbs ◽  
2021 ◽  
Vol 13 (1) ◽  
pp. 1893888
Author(s):  
Simone Mester ◽  
Mitchell Evers ◽  
Saskia Meyer ◽  
Jeannette Nilsen ◽  
Victor Greiff ◽  
...  
Keyword(s):  
Half Life ◽  
Binding Domain ◽  
Albumin Binding ◽  
Extended Plasma ◽  
Ph Dependent ◽  
Plasma Half Life

scholarly journals Enhancedin VivoEfficacy of a Type I Interferon Superagonist with Extended Plasma Half-life in a Mouse Model of Multiple Sclerosis

2014 ◽  
Vol 289 (42) ◽  
pp. 29014-29029 ◽  
Author(s):  
Daniel Harari ◽  
Nadine Kuhn ◽  
Renne Abramovich ◽  
Keren Sasson ◽  
Alla L. Zozulya ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Mouse Model ◽  
Half Life ◽  
Type I Interferon ◽  
Type I ◽  
Extended Plasma ◽  
Plasma Half Life

scholarly journals An engineered human albumin enhances half-life and transmucosal delivery when fused to protein-based biologics

2020 ◽  
Vol 12 (565) ◽  
pp. eabb0580
Author(s):  
Malin Bern ◽  
Jeannette Nilsen ◽  
Mattia Ferrarese ◽  
Kine M. K. Sand ◽  
Torleif T. Gjølberg ◽  
...  
Keyword(s):  
Half Life ◽  
Coagulation Factor ◽  
Human Albumin ◽  
Factor Vii ◽  
Coagulation Factor Vii ◽  
Activated Factor Vii ◽  
Extended Plasma ◽  
Albumin Variant ◽  
Transcellular Delivery ◽  
Plasma Half Life

Needle-free uptake across mucosal barriers is a preferred route for delivery of biologics, but the efficiency of unassisted transmucosal transport is poor. To make administration and therapy efficient and convenient, strategies for the delivery of biologics must enhance both transcellular delivery and plasma half-life. We found that human albumin was transcytosed efficiently across polarized human epithelial cells by a mechanism that depends on the neonatal Fc receptor (FcRn). FcRn also transported immunoglobulin G, but twofold less than albumin. We therefore designed a human albumin variant, E505Q/T527M/K573P (QMP), with improved FcRn binding, resulting in enhanced transcellular transport upon intranasal delivery and extended plasma half-life of albumin in transgenic mice expressing human FcRn. When QMP was fused to recombinant activated coagulation factor VII, the half-life of the fusion molecule increased 3.6-fold compared with the wild-type human albumin fusion, without compromising the therapeutic properties of activated factor VII. Our findings highlight QMP as a suitable carrier of protein-based biologics that may enhance plasma half-life and delivery across mucosal barriers.

Development and in vivo characterization of a novel peptide drug delivery system providing extended plasma half life

2012 ◽  
Vol 157 (3) ◽  
pp. 375-382 ◽  
Author(s):  
Gul Shahnaz ◽  
Javed Iqbal ◽  
Deni Rahmat ◽  
Glen Perera ◽  
Flavia Laffleur ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Drug Delivery System ◽  
Delivery System ◽  
Half Life ◽  
Peptide Drug ◽  
Extended Plasma ◽  
In Vivo Characterization ◽  
Plasma Half Life

Covalent Complexes Between Low Molecular Weight Heparin Fragments and Antithrombin III – Inhibition Kinetics and Turnover Parameters

1983 ◽  
Vol 49 (02) ◽  
pp. 109-115 ◽  
Author(s):  
M Hoylaerts ◽  
E Holmer ◽  
M de Mol ◽  
D Collen
Keyword(s):  
Molecular Weight ◽  
Half Life ◽  
Low Molecular Weight Heparin ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Life Time ◽  
Low Molecular Weight ◽  
High Affinity ◽  
Plasma Half Life ◽  
Covalent Complex

SummaryTwo high affinity heparin fragments (A/r 4,300 and M, 3,200) were covalently coupled to antithrombin III (J. Biol. Chem. 1982; 257: 3401-3408) with an apparent 1:1 stoichiometry and a 30-35% yield.The purified covalent complexes inhibited factor Xa with second order rate constants very similar to those obtained for antithrombin III saturated with these heparin fragments and to that obtained for the covalent complex between antithrombin III and native high affinity heparin.The disappearance rates from plasma in rabbits of both low molecular weight heparin fragments and their complexes could adequately be represented by two-compartment mammillary models. The plasma half-life (t'/j) of both low Afr-heparin fragments was approximately 2.4 hr. Covalent coupling of the fragments to antithrombin III increased this half-life about 3.5 fold (t1/2 ≃ 7.7 hr), approaching that of free antithrombin III (t1/2 ≃ 11 ± 0.4 hr) and resulting in a 30fold longer life time of factor Xa inhibitory activity in plasma as compared to that of free intact heparin (t1/2 ≃ 0.25 ± 0.04 hr).

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