scholarly journals Insight into purification of monoclonal antibodies in industrial columns via studies of Protein A binding capacity by in situ ATR-FTIR spectroscopy

The Analyst ◽  
2021 ◽  
Author(s):  
James Beattie ◽  
Ruth Rowland-Jones ◽  
Monika Farys ◽  
Richard Kucia-Tran ◽  
Sergei Kazarian ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Ftir Spectroscopy ◽  
Binding Capacity ◽  
Protein A ◽  
Therapeutic Monoclonal Antibodies ◽  
Insight Into ◽  
Effective Treatments

Therapeutic monoclonal antibodies (mAbs) are effective treatments for a range of cancers and other serious diseases, however mAb treatments cost on average ~$100,000 per year per patient, limiting their use....

Intracellular delivery of biomineralized monoclonal antibodies to combat viral infection

2016 ◽  
Vol 52 (9) ◽  
pp. 1879-1882 ◽  
Author(s):  
Zhiyong Song ◽  
Long Liu ◽  
Xiaoyu Wang ◽  
Yongqiang Deng ◽  
Qinggong Nian ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Viral Replication ◽  
Viral Infection ◽  
Intracellular Delivery ◽  
Therapeutic Monoclonal Antibodies

Conventional therapeutic monoclonal antibodies (mAbs) are invalid for intracellular viruses but by using in situ biomineralization treatment, they can be successfully delivered into cells to inhibit intracellular viral replication.

scholarly journals A Ligand-Directed Nitrophenol Carbonate for Transient In Situ Bioconjugation and Drug Delivery

2020 ◽  
Author(s):  
Anthony J. Burt ◽  
Parvaneh Ahmadvand ◽  
Larissa K. Opp ◽  
ChulHee Kang ◽  
Rock Mancini
Keyword(s):  
Active Drug ◽  
Immune Cell ◽  
Protein A ◽  
Model System ◽  
Time Dependent ◽  
Transient Nature ◽  
Directing Group ◽  
Self Immolation ◽  
Insight Into

Here we report the first use of ligand-directed proximity accelerated bioconjugation chemistry in the tandem delivery and release of a therapeutic payload. To do this we designed a nitrophenol carbonate for ligand-directed in situ bioconjugation of a prodrug payload to a protein. The transient nature of our conjugation chemistry renders the protein a depot for time-dependent release of active drug following hydrolysis and self-immolation. In our model system, using an immunostimulant prodrug, biotin ligand, and avidin protein, we observe time-dependent release of bioavailable immunostimulant both spectroscopically and with an immune cell line over 48 h. Avidin co-crystalized with the biotin directing group verified the binding pose of the ligand and offered insight into the mechanism of in situ bioconjugation. Overall, this scaffold warrants further investigation for the time-dependent delivery of therapeutics and use in protein ligand pairs beyond biotin and avidin used for this work.

FTIR spectroscopy as an analytical tool to compare glycosylation in therapeutic monoclonal antibodies

2020 ◽  
Vol 1112 ◽  
pp. 62-71 ◽  
Author(s):  
Allison Derenne ◽  
Kheiro-Mouna Derfoufi ◽  
Ben Cowper ◽  
Cédric Delporte ◽  
Erik Goormaghtigh
Keyword(s):  
Monoclonal Antibodies ◽  
Ftir Spectroscopy ◽  
Analytical Tool ◽  
Therapeutic Monoclonal Antibodies

Ultrastructural localization in host tissues of a toxic glycopeptide produced by Ophiostoma ulmi, using monoclonal antibodies

1985 ◽  
Vol 63 (7) ◽  
pp. 1185-1195 ◽  
Author(s):  
Nicole Benhamou ◽  
J. G. Lafontaine ◽  
J. R. Joly ◽  
G. B. Ouellette
Keyword(s):  
Monoclonal Antibodies ◽  
Protein A ◽  
Middle Lamella ◽  
Protective Layer ◽  
Ultrastructural Localization ◽  
Wall Layer ◽  
Dutch Elm Disease ◽  
Ophiostoma Ulmi

Monoclonal antibodies against a phytotoxic glycopeptide from Ophiostoma ulmi (Buism.) Nannf., the Dutch elm disease pathogen, were used in a postembedding protein A – gold labeling technique to localize this toxin in experimentally infected tissues of young elm seedlings. Significant labeling was observed over pit membranes, over the innermost wall layer (protective layer) of paratracheal parenchyma cells, and over the intercellular spaces and, adjacently, the middle lamella. Host secondary walls, cytoplasm, and various organelles, except regions of amyloplastids, were free of labeling. From day 1 to day 4 after inoculation an intensification of the labeling reaction was noted that corresponded to an increase in the disease symptoms. This specific and sensitive technique has thus proved to be highly suitable for the in situ identification of antigenic macromolecules in diseased elm tissues. The classification of the toxic glycopeptide among the group of vivotoxins is discussed.

scholarly journals A Ligand-Directed Nitrophenol Carbonate for Transient In Situ Bioconjugation and Drug Delivery

2020 ◽  
Author(s):  
Anthony J. Burt ◽  
Parvaneh Ahmadvand ◽  
Larissa K. Opp ◽  
ChulHee Kang ◽  
Rock Mancini
Keyword(s):  
Active Drug ◽  
Immune Cell ◽  
Protein A ◽  
Model System ◽  
Time Dependent ◽  
Transient Nature ◽  
Directing Group ◽  
Self Immolation ◽  
Insight Into

Here we report the first use of ligand-directed proximity accelerated bioconjugation chemistry in the tandem delivery and release of a therapeutic payload. To do this we designed a nitrophenol carbonate for ligand-directed in situ bioconjugation of a prodrug payload to a protein. The transient nature of our conjugation chemistry renders the protein a depot for time-dependent release of active drug following hydrolysis and self-immolation. In our model system, using an immunostimulant prodrug, biotin ligand, and avidin protein, we observe time-dependent release of bioavailable immunostimulant both spectroscopically and with an immune cell line over 48 h. Avidin co-crystalized with the biotin directing group verified the binding pose of the ligand and offered insight into the mechanism of in situ bioconjugation. Overall, this scaffold warrants further investigation for the time-dependent delivery of therapeutics and use in protein ligand pairs beyond biotin and avidin used for this work.

Plasminogen Activation In Vivo upon Intravenous Infusion of DDAVP

1992 ◽  
Vol 67 (01) ◽  
pp. 111-116 ◽  
Author(s):  
Marcel Levi ◽  
Jan Paul de Boer ◽  
Dorina Roem ◽  
Jan Wouter ten Cate ◽  
C Erik Hack
Keyword(s):  
Monoclonal Antibodies ◽  
Plasminogen Activator ◽  
Plasma Levels ◽  
Fold Increase ◽  
Fibrinolytic System ◽  
Plasminogen Activation ◽  
Plasminogen Activator Activity ◽  
Insight Into

SummaryInfusion of desamino-d-arginine vasopressin (DDAVP) results in an increase in plasma plasminogen activator activity. Whether this increase results in the generation of plasmin in vivo has never been established.A novel sensitive radioimmunoassay (RIA) for the measurement of the complex between plasmin and its main inhibitor α2 antiplasmin (PAP complex) was developed using monoclonal antibodies preferentially reacting with complexed and inactivated α2-antiplasmin and monoclonal antibodies against plasmin. The assay was validated in healthy volunteers and in patients with an activated fibrinolytic system.Infusion of DDAVP in a randomized placebo controlled crossover study resulted in all volunteers in a 6.6-fold increase in PAP complex, which was maximal between 15 and 30 min after the start of the infusion. Hereafter, plasma levels of PAP complex decreased with an apparent half-life of disappearance of about 120 min. Infusion of DDAVP did not induce generation of thrombin, as measured by plasma levels of prothrombin fragment F1+2 and thrombin-antithrombin III (TAT) complex.We conclude that the increase in plasminogen activator activity upon the infusion of DDAVP results in the in vivo generation of plasmin, in the absence of coagulation activation. Studying the DDAVP induced increase in PAP complex of patients with thromboembolic disease and a defective plasminogen activator response upon DDAVP may provide more insight into the role of the fibrinolytic system in the pathogenesis of thrombosis.

Design of Innovative Therapeutic Monoclonal Antibodies

2017 ◽  
pp. 10-29
Author(s):  
A.V. Karabelskii ◽  
◽  
T.A. Nemankin ◽  
A.B. Ulitin ◽  
A.S. Vaganov ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Therapeutic Monoclonal Antibodies

Rapid quantification and in situ detection of nitrifying bacteria in biofilms by monoclonal antibody method

2000 ◽  
Vol 41 (4-5) ◽  
pp. 301-308 ◽  
Author(s):  
N. Noda ◽  
H. Ikuta ◽  
Y. Ebie ◽  
A. Hirata ◽  
S. Tsuneda ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Fluorescent Antibody ◽  
Nitrifying Bacteria ◽  
Fluorescent Antibody Technique ◽  
Antibody Technique ◽  
Antibody Method ◽  
In Situ Detection ◽  
Rapid Quantification

Fluorescent antibody technique by the monoclonal antibody method is very useful and helpful for the rapid quantification and in situ detection of the specific bacteria like nitrifiers in a mixed baxterial habitat such as a biofilm. In this study, twelve monoclonal antibodies against Nitrosomonas europaea (IFO14298) and sixteen against Nitrobacter winogradskyi (IFO14297) were raised from splenocytes of mice (BALB/c). It was found that these antibodies exhibited little cross reactivity against various kinds of heterotrophic bacteria. The direct cell count method using monoclonal antibodies could exactly detect and rapidly quantify N. europaea and N. winogradskyi. Moreover, the distribution of N. europaea and N. winogradskyi in a biofilm could be examined by in situ fluorescent antibody technique. It was shown that most of N. winogradskyi existed near the surface part and most of N. europaea existed at the inner part of the polyethylene glycol (PEG) gel pellet, which had entrapped activated sludge and used in a landfill leachate treatment reactor. It was suggested that this monoclonal antibody method was utilized for estimating and controlling the population of nitrifying bacteria as a quick and favorable tool.

Therapeutic Monoclonal Antibodies in Clinical Practice against Cancer

2020 ◽  
Vol 20 (16) ◽  
pp. 1895-1907
Author(s):  
Navgeet Kaur ◽  
Anju Goyal ◽  
Rakesh K. Sindhu
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Clinical Practice ◽  
Therapeutic Agent ◽  
Hematologic Malignancies ◽  
Immune Checkpoints ◽  
Malignant Cells ◽  
Main Target ◽  
Therapeutic Monoclonal Antibodies ◽  
Cancerous Cells

The importance of monoclonal antibodies in oncology has increased drastically following the discovery of Milstein and Kohler. Since the first approval of the monoclonal antibody, i.e. Rituximab in 1997 by the FDA, there was a decline in further applications but this number has significantly increased over the last three decades for various therapeutic applications due to the lesser side effects in comparison to the traditional chemotherapy methods. Presently, numerous monoclonal antibodies have been approved and many are in queue for approval as a strong therapeutic agent for treating hematologic malignancies and solid tumors. The main target checkpoints for the monoclonal antibodies against cancer cells include EGFR, VEGF, CD and tyrosine kinase which are overexpressed in malignant cells. Other immune checkpoints like CTLA-4, PD-1 and PD-1 receptors targeted by the recently developed antibodies increase the capability of the immune system in destroying the cancerous cells. Here, in this review, the mechanism of action, uses and target points of the approved mAbs against cancer have been summarized.

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