Selection of cholera toxin specific IgNAR single-domain antibodies from a naïve shark library

Improving the pharmacokinetic properties of biologics by fusion to an anti-HSA shark VNAR domain

“…43 It has been well established that IgNAR is amenable to phage display-immunized, naïve and semi-synthetic IgNAR phage display libraries have been reported in the literature. 42,[45][46][47][48][49][50] Here too, it proved an effective platform for the iterative enrichment and isolation of antigen specific binders. As serum albumin binds in a pH-dependent manner to FcRn, it was critical to incorporate this parameter in the post-selection characterization of lead clones in addition to cross-reactivity with MSA to fit with our initial murine PK model.…”

The rational development of molecularly imprinted polymer-based sensors for protein detection

“…Whilst these bio-molecules fulfil the requirements of specificity, selectivity and ease of use, such as the ability to absorb or chemically couple to solid surfaces with little denaturation, 4 they have limited stability to extremes of temperature (denaturing above ~40 ºC) and humidity as well susceptibility to damage by shear forces, such as those encountered in continuous monitoring situations. Recent efforts have included studies with antibodies and antibody fragments from camelids such as the llama 5 or from sharks 6 to overcome some of these issues. These antibodies differ from conventional IgG since they consist of only a single heavy chain which imparts greater temperature stability without sacrificing specificity or selectivity.…”

Nanobody-derived nanobiotechnology tool kits for diverse biomedical and biotechnology applications

“…1,5,9 Therefore, to some extent, the nanobodies (VHHs or V-NARs) with a molecular weight of ~12-15 kDa in the HCAbs or IgNARs are the structural and functional counterparts of the Fabs in the conventional IgGs ( Figure 1B, E, and H). 1,3,5,8 Similar to the VH domain in conventional IgGs, the folded VHH in camel HCAbs comprises nine β-strands. These β-strands, organized in a four-stranded β-sheet and a five-stranded β-sheet, were connected by three hypervariable (HV) loops, also called complementarity-determining regions (CDRs), and by a conserved disulfide bond between Cys23 within framework region (FR) 1 and Cys94 within FR3.…”

“…1 Some cartilaginous fish, including nurse shark (Ginglymostoma cirratum), wobbegong (Orectolobus maculates), and dogfish (Squalus acanthias and Mustelus canis) sharks, also remarkably produce functional heavychain-only immunoglobulins (Igs), named IgNARs. 1,[5][6][7][8] Interestingly, some pathological and nonfunctional HCAbs were also discovered in sera of humans or in mouse hybridoma due to a partly genetic deletion of the variable heavychain (VH) and CH1 regions. 1 In camels or sharks, these HCAbs (or IgNARs) recognize the antigens via single variable domains, referred to as VHHs or V-NARs, respectively.…”

“…Owing to the small dimensional size of 2.5 nm in diameter and 4 nm in height (~12-15 kDa), Ablynx in 2003 dubbed these sdAbs "nanobody" to emphasize their smaller dimensional sizes, compared to larger molecular sizes of single-chain variable fragments (scFvs; 27 kDa), antigenbinding fragments (Fabs; ~57kDa), and the intact conventional immunoglobulin-γ (IgG) antibody (~150 kDa). 3,5,8 In this review, we summarize the current state of the art in nanobody research, focusing on the nanobody structural features, nanobody production approach, nanobody-derived nanobiotechnology tool kits, and the potential applications in biomedicine and biotechnology.…”