Avidin-biotin technology in targeted therapy

Lesch, Hanna P.; Kaikkonen, Minna U.; Pikkarainen, Jere T.; Ylä‐Herttuala, Seppo

doi:10.1517/17425241003677749

Cited by 171 publications

(137 citation statements)

References 86 publications

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“…These discrete self-assembly processes are the basis for different applications in histology, imaging, diagnosis, catalysis, analysis, and purification. 1,2,3,4 …”

Section: Background On Biotin/(strept)avidinmentioning

confidence: 99%

Synthetic mimics of biotin/(strept)avidin

et al. 2017

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Biotin/(strept)avidin self-assembly is a powerful platform for nanoscale fabrication and capture with many different applications in science, medicine, and nanotechnology. However, biotin/(strept)avidin self-assembly has several well-recognized drawbacks that limit performance in certain technical areas and there is a need for synthetic mimics that can either become superior replacements or operational partners with bio-orthogonal recognition properties. The goal of this tutorial review is to describe the recent progress in making high affinity synthetic association partners that operate in water or biological media. The review starts with a background summary of biotin/(strept)avidin self-assembly and the current design rules for creating synthetic mimics. A series of case studies are presented that describe recent success using synthetic derivatives of cyclodextrins, cucurbiturils, and various organic cyclophanes such as calixarenes, deep cavitands, pillararenes, and tetralactams. In some cases, two complementary partners associate to produce a nanoscale complex and in other cases a ditopic host molecule is used to link two partners. The article concludes with a short discussion of future directions and likely challenges.

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“…These discrete self-assembly processes are the basis for different applications in histology, imaging, diagnosis, catalysis, analysis, and purification. 1,2,3,4 …”

Section: Background On Biotin/(strept)avidinmentioning

confidence: 99%

Synthetic mimics of biotin/(strept)avidin

et al. 2017

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“…Avidins are known to be homotetrametric proteins, with the exception rhizavidin, which is a homodimer in its native form [11]. Due to the high-affinity interaction with D-biotin, avidins are widely applied in life sciences as well as in bio- and nanotechnology [13]–[15].…”

Section: Introductionmentioning

confidence: 99%

Structure of Bradavidin – C-Terminal Residues Act as Intrinsic Ligands

et al. 2012

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Bradavidin is a homotetrameric biotin-binding protein from Bradyrhizobium japonicum, a nitrogen fixing and root nodule-forming symbiotic bacterium of the soybean. Wild-type (wt) bradavidin has 138 amino acid residues, whereas the C-terminally truncated core-bradavidin has only 118 residues. We have solved the X-ray structure of wt bradavidin and found that the C-terminal amino acids of each subunit were uniquely bound to the biotin-binding pocket of an adjacent subunit. The biotin-binding pocket occupying peptide (SEKLSNTK) was named “Brad-tag” and it serves as an intrinsic stabilizing ligand in wt bradavidin. The binding of Brad-tag to core-bradavidin was analysed by isothermal titration calorimetry and a binding affinity of ∼25 µM was measured. In order to study the potential of Brad-tag, a green fluorescent protein tagged with Brad-tag was prepared and successfully concentrated from a bacterial cell lysate using core-bradavidin-functionalized Sepharose resin.

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“…Owing to the superb affinity (Kd = 10 -15 M) and stability of streptavidinbiotin binding, this reaction has been used in previous studies for targeting viral and nonviral vectors, as well as other cargo, to various cell types [66][67][68][69]. It offers considerable advantages over other adaptor systems, affording outstanding stability of targeted materials.…”

Section: Discussionmentioning

confidence: 99%

Low-Affinity Neurotrophin Receptor p75 Promotes the Transduction of Targeted Lentiviral Vectors to Cholinergic Neurons of Rat Basal Forebrain

et al. 2016

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Basal forebrain cholinergic neurons (BFCNs) are one of the most affected neuronal types in Alzheimer's disease (AD), with their extensive loss documented at late stages of the pathology. While discriminatory provision of neuroprotective agents and trophic factors to these cells is thought to be of substantial therapeutic potential, the intricate topography and structure of the forebrain cholinergic system imposes a major challenge. To overcome this, we took advantage of the physiological enrichment of BFCNs with a low-affinity p75 neurotrophin receptor (p75 NTR ) for their targeting by lentiviral vectors within the intact brain of adult rat. Herein, a method is described that affords selective and effective transduction of BFCNs with a green fluorescence protein (GFP) reporter, which combines streptavidinbiotin technology with anti-p75 NTR antibody-coated lentiviral vectors. Specific GFP expression in cholinergic neurons was attained in the medial septum and nuclei of the diagonal band Broca after a single intraventricular administration of such targeted vectors. Bioelectrical activity of GFP-labeled neurons was proven to be unchanged. Thus, proof of principle is obtained for the utility of the lowaffinity p75 NTR for targeted transduction of vectors to BFCNs in vivo.

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Avidin-biotin technology in targeted therapy

Abstract: Avidin and biotin technology has proved to be an extremely versatile tool with broad applications, such as pretargeting, delivering avidin gene into cells enabling targeting of biotinylated compounds and targeting of viral vectors.

Cited by 171 publications

References 86 publications

Synthetic mimics of biotin/(strept)avidin

Synthetic mimics of biotin/(strept)avidin

Structure of Bradavidin – C-Terminal Residues Act as Intrinsic Ligands

Low-Affinity Neurotrophin Receptor p75 Promotes the Transduction of Targeted Lentiviral Vectors to Cholinergic Neurons of Rat Basal Forebrain

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