Dissociation constant of the streptavidin and biotin interaction (highest affinity among naturally occurring non-covalent bonds)

Range 10^-13 - 10^-16 M
Organism Generic
Reference Park M et al., Orientation and density control of proteins on solid matters by outer membrane coating: Analytical and diagnostic applications. J Pharm Biomed Anal. 2017 Jul 31. pii: S0731-7085(17)31544-3. doi: 10.1016/j.jpba.2017.07.043 p.3 left column top paragraphPubMed ID28797956
Primary Source [45] Green NM. Avidin. Adv Protein Chem. 1975 29: 85-133.PubMed ID237414
Comments P.3 left column top paragraph: "Avidin and streptavidin are two additional affinity proteins, commonly used in biomedical applications. Avidin is a 66–69-kDa tetrameric protein found in the egg white of birds, reptiles, and amphibians [refs 44, 46, primary source]. Streptavidin is found in Streptomyces avidinii, and both avidin and streptavidin show affinity for biotin, also known as vitamin B7 or vitamin H [ref 44, primary source]. Streptavidin is a tetrameric protein with eight antiparallel β-strands and each subunit contains a biotin-binding site [refs 47,48]. Based on thise structural consideration, a monomeric streptavidin was developed with similar binding affinity to biotin [refs 49,50]. The dissociation constant of the streptavidin and biotin interaction is 10^13–10^16 M and shows the highest affinity among naturally occurring non-covalent bonds [primary source]. This interaction is mediated not only by hydrogen bonds, but also included a substantial portion of hydrophobic interactions [ref 48]. This strong binding is pseudo-irreversible as well as durable in the presence of organic solvents, detergents, pH, and high temperature. To exploit the strong bonding between biotin-streptavidin, various biotinylation strategies were developed [refs 51–54]."
Entered by Uri M
ID 114157