title: Improvement of single domain antibody stability by disulfide bond introduction.
abstract: The successful medical application of single domain antibodies largely depends on their functionality. This feature is partly determined by the intrinsic stability of the single domain. Therefore a lot of research has gone into the elucidation of rules to uniformly increase stability of antibodies. Recently, a novel intra-domain disulfide bond was independently discovered by two research groups, after either rational design or careful investigation of the naturally occurring camelid antibody repertoire. By introducing this particular disulfide bond within a single domain antibody, the conformational stability can be increased in general. In this chapter it is described how to introduce this extra intra-domain disulfide bond and how to estimate the biophysical and biochemical impact of this cystine on the domain.
authors.affiliation: National Institute of Advanced Industrial Science and Technology (AIST), Ikeda, Osaka, Japan. hagihara-kappael@aist.go.jp
authors.forename: Yoshihisa
authors.initials: Y
authors.lastname: Hagihara
authors.forename: Dirk
authors.initials: D
authors.lastname: Saerens
mesh_terms: D000595:Amino Acid Sequence; D000915:Antibody Affinity; D004220:Disulfides / Q000737:chemistry*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011489:Protein Denaturation; D015202:Protein Engineering; D017510:Protein Folding; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D061905:Single-Domain Antibodies / Q000737:chemistry* / Q000235:genetics; D013696:Temperature
chemical_list: D004220:Disulfides; D061905:Single-Domain Antibodies