Results 11 to 20 of about 8,345 (257)
Engineering the fragment crystallizable (Fc) region of human IgG1 multimers and monomers to fine-tune interactions with sialic acid-dependent receptors [PDF]
Multimeric fragment crystallizable (Fc) regions and Fc-fusion proteins are actively being explored as biomimetic replacements for IVIG therapy, which is deployed to manage many diseases and conditions but is expensive and not always efficient. The Fc region of human IgG1 (IgG1-Fc) can be engineered into multimeric structures (hexa-Fcs) that bind their ...
Patricia A. Blundell +4 more
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Non-covalent Fc-Fab interactions significantly alter internal dynamics of an IgG1 antibody
The fragment-antigen-binding arms (Fab1 and Fab2) in a canonical immunoglobulin G (IgG) molecule have identical sequences and hence are always expected to exhibit symmetric conformations and dynamics.
Ramakrishnan Natesan, Neeraj J. Agrawal
doaj +1 more source
Post-translational modifications (PTMs) of therapeutic monoclonal antibodies (mAbs) can impact the efficacy of a drug. Methionine oxidation can alter the overall hydrophobicity of an antibody, thereby inducing conformational changes and affecting its ...
Somar Khalil +6 more
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Modified Therapeutic Antibodies: Improving Efficacy
The prosperity of the biotherapeutics market reflects the feasibility and effectiveness of therapeutic antibodies for the treatment of cancers, inflammatory disorders, and refractory infections.
Ji-Min Dai +4 more
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We previously reported a new polymer, lactic-co-glycolic acid-polyethylenimine (LGA-PEI), as an improved nanoparticle (NP) delivery for therapeutic nucleic acids (TNAs).
Jian-Ming Lü +5 more
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The function of antibodies, namely the identification and neutralization of pathogens, is mediated by their antigen binding site (Fab). In contrast, the subsequent signal transduction for activation of the immune system is mediated by the fragment ...
Kristina Zlatina, Sebastian P. Galuska
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A Method to Detect the Binding of Hyper-Glycosylated Fragment Crystallizable (Fc) Region of Human IgG1 to Glycan Receptors [PDF]
Engineering the fragment crystallizable (Fc) of human IgG can bring improved effector functions to monoclonal antibodies and Fc-fusion-based medicines and vaccines. Such Fc-effector functions are largely controlled by posttranslational modifications (PTMs) within the Fc, including the addition of glycans that introduce structural and functional ...
Patricia, Blundell, Richard, Pleass
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Mycobacterium tuberculosis (Mtb) infects one-quarter of the world's population. Mtb and HIV coinfections enhance the comorbidity of tuberculosis (TB) and AIDS, accounting for one-third of all AIDS-associated mortalities.
Hui-Chen Chang Foreman +2 more
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Generating Recombinant Antibodies against Putative Biomarkers of Retinal Injury. [PDF]
Candidate biomarkers, indicative of disease or injury, are beginning to overwhelm the process of validation through immunological means. Recombinant antibodies developed through phage-display offer an alternative means of generating monoclonal antibodies
Michael R Kierny +4 more
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Choice of host cell line is essential for the functional glycosylation of the fragment crystallizable (Fc) region of human IgG1 inhibitors of influenza B viruses [PDF]
AbstractAntibodies are glycoproteins that carry a conserved N-linked carbohydrate attached to the Fc, whose presence and fine structure profoundly impacts on theirin vivoimmunogenicity, pharmacokinetics and functional attributes. The host cell line used to produce IgG has a major impact on this glycosylation, as different systems express different ...
Blundell, Patricia A. +4 more
openaire +1 more source

