Single-domain antibody fragments with high conformational stability

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Single-domain antibody fragments with high conformational stability.

A variety of techniques, including high-pressure unfolding monitored by Fourier transform infrared spectroscopy, fluorescence, circular dichroism, and surface plasmon resonance spectroscopy, have been used to investigate the equilibrium folding properties of six single-domain antigen binders derived from camelid heavy-chain antibodies with specificities for lysozymes, beta-lactamases, and a dye...

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The application of single-chain Fv fragments (scFv) in medicine and biotechnology places great demands on their stability. Only recently has attention been given to the production of highly stable scFvs, and in a number of examples it was found that such fragments indeed perform better during practical applications. The structural parameters influencing scFv stability are now beginning to be el...

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Biotechnological applications of recombinant single-domain antibody fragments

BACKGROUND Single-domain antibody fragments possess structural features, such as a small dimension, an elevated stability, and the singularity of recognizing epitopes non-accessible for conventional antibodies that make them interesting for several research and biotechnological applications. RESULTS The discovery of the single-domain antibody's potentials has stimulated their use in an increa...

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Controlling Rotavirus-associated diarrhea: Could single-domain antibody fragments make the difference?

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Small, soluble single-domain fragments derived from the unique variable region of dromedary heavy-chain antibodies (VHHs) against enzymes are known to be potent inhibitors. The immunization of dromedaries with the TEM-1 and BcII beta-lactamases has lead to the isolation of such single-domain antibody fragments specifically recognizing and inhibiting those beta-lactamases. Two VHHs were isolated...

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ژورنال

عنوان ژورنال: Protein Science

سال: 2009

ISSN: 0961-8368

DOI: 10.1110/ps.34602