Molecular recognition requires dimerization of a VHH antibody
MAbs, 2023 Camelid heavy-chain-only antibodies are a unique class of antibody that possesses only a single variable domain (termed VHH) for antigen recognition.
Andrew Herr, James R Horn
exaly +5 more sources
VHH characterization. Comparison of recombinant with chemically synthesized anti‐HER2 VHH [PDF]
Protein Science, 2019 AbstractIn the continuous exploration of the VHH chemistry, biochemistry and therapeutic future use, we investigated two different production strategies of this small antibody‐like protein, using an anti‐HER2 VHH as a model. The total chemical synthesis of the 125 amino‐acid peptide was performed with reasonable yield, even if optimization will be ...
Renaud Wagner +2 more
exaly +4 more sources
Bispecific single-domain antibody (VHH) fused with human IgG1 Fc with dual specificity effectively neutralize Naja Kaouthia venom. [PDF]
PLoS Neglected Tropical DiseasesNaja kaouthia, or the monocled cobra, is one of the most medically important snakes in Thailand, responsible for approximately 17% of snakebite cases. Conventional horse-derived antivenoms are lifesaving, yet they may trigger severe allergic reactions ...
Kanokporn Pothisamutyothin +4 more
doaj +2 more sources
VHH Antibodies: Reagents for Mycotoxin Detection in Food Products
Sensors, 2018 Mycotoxins are the toxic secondary metabolites produced by fungi and they are a worldwide public health concern. A VHH antibody (or nanobody) is the smallest antigen binding entity and is produced by heavy chain only antibodies.
Jia Wang, Xiaohong Wang
exaly +3 more sources
Contribution of CDR3 in characterization of camelid VHH and its aflatoxin B1-binding interaction
Food Chemistry AdvancesThe single variable domain of heavy chain (VHH) antibodies, owing to their unique properties, has gained attention in immunoassays. However, compared with macromolecule antigens, in the case of small molecule haptens, such as aflatoxin B1 (AFB1), the ...
Jia Wang
exaly +3 more sources
Complete Neutralization of Tetanus Neurotoxin by Alpaca-Derived Trivalent Nanobodies Aimed at Veterinary Medical Applications [PDF]
Veterinary SciencesTetanus is a zoonotic disease posing significant threats to both humans and animals, particularly horses, sheep, and ruminants. Current antitoxin therapies rely on animal-derived immunoglobulins, presenting challenges including animal welfare concerns ...
Chiyomi Sakamoto +8 more
doaj +2 more sources
VHH-based CAR-T cells targeting Claudin 18.2 show high efficacy in pancreatic cancer models [PDF]
Frontiers in ImmunologyBackgroundPancreatic ductal adenocarcinoma (PDAC) remains one of the deadliest cancers, with a 5-year survival rate below 10%, largely due to late-stage diagnosis and the limited effectiveness of conventional therapies such as surgery, chemotherapy, and ...
Ying Xing +20 more
doaj +2 more sources
Molecular docking study and mapping the binding site of some antiviral nanobodies against receptor binding domain (RBD) of SARS-COV 2 [PDF]
Nanochemistry Research, 2021 Neutralization ability of some antiviral nanobodies was computed against the receptor binding domain (RBD) of the severe acute respiratory syndrome coronavirus 2 (SARS-COV 2).
zahra pahlavan, Mohammad Hossein Fatemi
doaj +1 more source
From discovery to the clinic: structural insights, engineering options, clinical, and ‘next wave’ applications of camelid-derived single-domain antibodies [PDF]
mAbsCamelid-derived single domain antibodies (sdAbs), referred to as VHHs (variable domains of the heavy chain of a heavy chain-only antibodies), recently emerged as promising building blocks for the construction of therapeutic molecules. As of October 2025,
Andreas Evers +3 more
doaj +2 more sources
VHH characterization.Recombinant VHHs: Production, characterization and affinity [PDF]
Analytical Biochemistry, 2020 Among the biological approaches to therapeutics, are the cells, such as CAR-T cells engineered or not, the antibodies armed or not, and the smaller protein scaffolds that can be modified to render them specific of other proteins, à la façon of antibodies.
Chabrol, Eric +8 more
openaire +3 more sources