Results 41 to 50 of about 41,395 (219)
Llama nanoantibodies with therapeutic potential against human norovirus diarrhea. [PDF]
PLoS ONE, 2015 Noroviruses are a major cause of acute gastroenteritis, but no vaccines or therapeutic drugs are available. Llama-derived single chain antibody fragments (also called VHH) are small, recombinant monoclonal antibodies of 15 kDa with several advantages ...
Lorena Garaicoechea +8 more
doaj +1 more source
VHH CDR-H3 conformation is determined by VH germline usage
Communications Biology, 2023 VHHs or nanobodies are single antigen binding domains originating from camelid heavy-chain antibodies. They are used as diagnostic and research tools and in a variety of therapeutic molecules. Analyzing variable domain structures from llama and alpaca we
Zahra Bahrami Dizicheh +2 more
semanticscholar +1 more source
Materials Today Chemistry, 2023 SARS-CoV-2 rapid spread required urgent, accurate, and prompt diagnosis to control the virus dissemination and pandemic management. Several sensors were developed using different biorecognition elements to obtain high specificity and sensitivity. However,
A. Santos +17 more
semanticscholar +1 more source
Isolation of Novel EGFR-Specific VHH Domains [PDF]
SLAS Discovery, 2009 Epidermal growth factor receptor (EGFR) is overexpressed or mutated in a high percentage of tumors. EGFR has long been considered a promising target for cancer diagnostic and therapeutic applications. However, monoclonal antibodies and other large antibody constructs diffuse into tumors slowly, limiting their efficacy. To develop lower molecular weight
Elizabeth B, Gottlin +5 more
openaire +2 more sources
Development of VHH antibodies against dengue virus type 2 NS1 and comparison with monoclonal antibodies for use in immunological diagnosis. [PDF]
PLoS ONE, 2014 The possibility of using variable domain heavy-chain antibodies (VHH antibodies) as diagnostic tools for dengue virus (DENV) type 2 NS1 protein was investigated and compared with the use of conventional monoclonal antibodies.
Aneela Fatima +7 more
doaj +1 more source
Accelerating GPCR Drug Discovery With Conformation-Stabilizing VHHs
Frontiers in Molecular Biosciences, 2022 The human genome encodes 850 G protein-coupled receptors (GPCRs), half of which are considered potential drug targets. GPCRs transduce extracellular stimuli into a plethora of vital physiological processes. Consequently, GPCRs are an attractive drug target class.
Toon Laeremans +10 more
openaire +3 more sources
mAbs, 2023 As small and stable high-affinity antigen binders, VHHs boast attractive characteristics both for therapeutic use in various disease indications, and as versatile reagents in research and diagnostics.
Loes van Schie +15 more
semanticscholar +1 more source
DISCOVERY OF NOVEL ANTI-SERUM ALBUMIN VHH AS A BUILDING BLOCK FOR PK PROLONGATION
Antibody Therapeutics, 2023 Background The serum half-life of endogenous albumin is approximately 19 days in humans and 1.5-2.5 days in rodents. This extended half-life in vivo is primarily due to effective recycling upon internalization mediated by the neonatal Fc receptor (FcRn).
Yunying Chen +5 more
semanticscholar +1 more source
Evaluation of the Potential Impact of In Silico Humanization on VHH Dynamics
International Journal of Molecular Sciences, 2023 Camelids have the peculiarity of having classical antibodies composed of heavy and light chains as well as single-chain antibodies. They have lost their light chains and one heavy-chain domain.
Carla Martins +3 more
semanticscholar +1 more source
Lactobacillli expressing llama VHH fragments neutralise Lactococcusphages [PDF]
BMC Biotechnology, 2007 Abstract Background Bacteriophages infecting lactic acid bacteria (LAB) are widely acknowledged as the main cause of milk fermentation failures. In this study, we describe the surface-expression as well as the secretion of two functional llama heavy-chain antibody fragments, one binding to the major capsid protein ...
Moineau Sylvain +6 more
openaire +3 more sources