
Simplified monomeric VHH-Fc antibodies provide new ... - PubMed
Simplified monomeric monoclonal antibodies consisting of a single-domain VHH, derived from camelid heavy-chain only antibodies, fused with the Fc domain of either IgG (VHH-IgG) or IgA (VHH-IgA) antibodies, are promising therapeutic proteins.
First-in-class trispecific VHH-Fc based antibody with potent ...
2022年3月9日 · Here, we evaluated in vivo efficacy and safety of the lead trispecific VHH-Fc, ABS-VIR-001. Importantly, our data showed that ABS-VIR-001 treatment prevented SARS-CoV-2 infection and death when...
Simplified monomeric VHH-Fc antibodies provide new opportunities for ...
2020年2月1日 · Simplified monomeric monoclonal antibodies consisting of a single-domain VHH, derived from camelid heavy-chain only antibodies, fused with the Fc domain of either IgG (VHH-IgG) or IgA (VHH-IgA) antibodies, are promising therapeutic proteins.
Development and characterization of a camelid derived antibody ...
2022年7月16日 · PCSK9 is an effective target for lowering LDL-c. Previously, a camelid-human chimeric heavy chain antibody VHH-B11-Fc targeting human PCSK9 was designed. It had a potent hypolipidemic effect....
Camelid VHHs Fused to Human Fc Fragments Provide Long Term …
We demonstrated that modification of neutralizing VHHs with a human immunoglobulin G (IgG)1 Fc (fragment crystallizable) fragment (fusionbody, VHH-Fc) significantly increased the circulation time in the blood (up to 14 days). At the same time, VHH-Fc showed the protective activity 1000 times higher than monomeric form when challenged with 5 LD ...
Fusion of an Fc chain to a VHH boosts the accumulation levels in ...
2013年8月6日 · Fusion of a ‘fragment crystallizable’ chain (Fc chain) of an antibody to the VHH domain results in a VHH-Fc fusion protein, and due to the Fc auto-oligomerization based on the disulphide bridges in the hinge region, a stable bivalent homodimeric complex is formed.
Fusion of an Fc chain to a VHH boosts the accumulation levels in ...
Nanobodies® (VHHs) provide powerful tools in therapeutic and biotechnological applications. Nevertheless, for some applications, bivalent antibodies perform much better, and for this, an Fc chain can be fused to the VHH domain, resulting in a bivalent homodimeric VHH-Fc complex.
Fusion of hIgG1-Fc to 111In-anti-amyloid single domain ... - PubMed
The fusion protein showed homodimerization - necessary for successful Fc neonatal receptor recycling. Compared to VHH-pa2H, the Fc tailed protein retained high affinity for amyloid beta on human AD patient brain tissue sections, and significantly improved serum retention of the VHH.
A VHH-Fc Fusion Targeted to the Chloroplast Thylakoid Lumen …
2021年5月28日 · Chimeric fusion proteins comprising a single domain antibody (V H H) fused to a crystallizable fragment (Fc) of an immunoglobulin are modular glycoproteins that are becoming increasingly in demand because of their value as diagnostics, research reagents and passive immunization therapeutics.
VHH single-domain platform enabling discovery and …
2024年5月3日 · A heavy chain-only tetravalent VHH-Fc-VHH bispecific platform derived from humanized synthetic libraries held a myriad of unique advantages: (i) synthetic preconstructed libraries minimized risk of liabilities and maximized discovery speed, (ii) VHH scaffolds allowed for a modular “plug-and-play” format that could be rapidly iterated upon ...