Strong supramolecular control over protein self-assembly using a polyamine decorated β-cyclodextrin as synthetic recognition element

Uhlenheuer, DA Dana; Milroy, L.-G.; Neirynck, Pauline; Brunsveld, Luc

doi:10.1039/c1jm12736e

Cited by 17 publications

(10 citation statements)

References 33 publications

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“…Amine-functionalized CD 1 is av ersatile scaffold, which has been used for the design of fluorescent sensors, [10,45] synthetic receptors, [46] investigated as ap recursor to forming glycoclusters, [47] controlling protein self-assembly, [48] DNA transfection, [49] and as an inhibitor of anthraxl ethal toxin. [50][51][52][53] In these examples, the amine groups of 1 were either per-functionalized, or monofunctionalized nonselectively with desired reagents.…”

Section: Introductionmentioning

confidence: 99%

Access to Versatile β‐Cyclodextrin Scaffolds through Guest‐Mediated Monoacylation

Vurgun

Gómez‐Biagi

Nitz

2015

Chemistry A European J

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Herein, we report the selective mono-derivatization of heptakis[6-deoxy-6-(2-aminoethylsulfanyl)]-β-CD (1) through a guest-mediated covalent capture strategy. The use of guests functionalized with cleavable linkers enables the installation of an amine-orthogonal thiol group on the primary rim of 1 as a handle for further transformations to the β-CD scaffold. Applying this methodology, two novel monoderivatized β-CDs were obtained in good yield and high purity. Both of these monoacylated CDs were amenable to facile linker cleavage and further modification at the resulting thiol group. This methodology can be applied towards the synthesis heterofunctionalized β-CD constructs for analyte sensing, drug delivery, and other applications.

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Section: Introductionmentioning

confidence: 99%

Access to Versatile β‐Cyclodextrin Scaffolds through Guest‐Mediated Monoacylation

Vurgun

Gómez‐Biagi

Nitz

2015

Chemistry A European J

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“…Most of these approaches rely on multivalent interactions of multiple guest molecules often randomly attached to the protein of interest; this makes molecular control and uniformity more difficult to achieve. Recently, we reported how expressed protein ligation can be used for the site‐selective incorporation of single host or guest elements into proteins,17–20 including a ferrocene unit and the reversible immobilization of this ferrocene conjugated protein on a cucurbituril surface 21. Site‐selective and monofunctional conjugation of host or guest tags offers distinct advantages over random protein labeling and new and versatile methods to incorporate supramolecular elements are therefore urgently needed.…”

Section: Introductionmentioning

confidence: 99%

Directed Supramolecular Surface Assembly of SNAP‐tag Fusion Proteins

Uhlenheuer

Wasserberg

Haase

et al. 2012

Chemistry A European J

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Supramolecular assembly of proteins on surfaces and vesicles was investigated by site-selective incorporation of a supramolecular guest element on proteins. Fluorescent proteins were site-selectively labeled with bisadamantane by SNAP-tag technology. The assembly of the bisadamantane functionalized SNAP-fusion proteins on cyclodextrin-coated surfaces yielded stable monolayers. The binding of the fusion proteins is specific and occurs with an affinity in the order of 10(6) M(-1) as determined by surface plasmon resonance. Reversible micropatterns of the fusion proteins on micropatterned cyclodextrin surfaces were visualized by using fluorescence microscopy. Furthermore, the guest-functionalized proteins could be assembled out of solution specifically onto the surface of cyclodextrin vesicles. The SNAP-tag labeling of proteins thus allows for assembly of modified proteins through a host-guest interaction on different surfaces. This provides a new strategy in fabricating protein patterns on surfaces and takes advantage of the high labeling efficiency of the SNAP-tag with designed supramolecular elements.

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“…Although this binding affinity could be influenced by attached proteins, we identified LA as an ideal affinity handle for the quantitative capture of modified proteins. However, the extremely low solubility of LA in water (0.05 μ m at 25 °C) has complicated direct bioconjugation, and so far only very few examples of synthetically attaching LA to proteins have been demonstrated . In these studies, green fluorescent protein derivatives were C‐terminally modified through expressed protein ligation—a technique that is not directly transferable to many proteins.…”

Section: Figurementioning

confidence: 99%

Capture and Recycling of Sortase A through Site‐Specific Labeling with Lithocholic Acid

et al. 2016

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Enzyme-mediated protein modification often requires large amounts of biocatalyst, adding significant costs to the process and limiting industrial applications. Herein, we demonstrate a scalable and straightforward strategy for the efficient capture and recycling of enzymes using a small-molecule affinity tag. A proline variant of an evolved sortase A (SrtA 7M) was N-terminally labeled with lithocholic acid (LA)-an inexpensive bile acid that exhibits strong binding to β-cyclodextrin (βCD). Capture and recycling of the LA-Pro-SrtA 7M conjugate was achieved using βCD-modified sepharose resin. The LA-Pro-SrtA 7M conjugate retained full enzymatic activity, even after multiple rounds of recycling.

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Strong supramolecular control over protein self-assembly using a polyamine decorated β-cyclodextrin as synthetic recognition element

Cited by 17 publications

References 33 publications

Access to Versatile β‐Cyclodextrin Scaffolds through Guest‐Mediated Monoacylation

Access to Versatile β‐Cyclodextrin Scaffolds through Guest‐Mediated Monoacylation

Directed Supramolecular Surface Assembly of SNAP‐tag Fusion Proteins

Capture and Recycling of Sortase A through Site‐Specific Labeling with Lithocholic Acid

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