cBSA-147 for the preparation of bacterial biofilms in a microchannel reactor

Ng, Jeck Fei; Jaenicke, Stephan; Eisele, Klaus; Dorn, Jan; Weil, Tanja

doi:10.1116/1.3474475

Cited by 11 publications

(11 citation statements)

References 23 publications

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“…Subsequent reaction with a diamine leads to a replacement of COO − for NH 3 + and an increase of two net charges at the reaction site ( N total : −1 to +1 = +2). Several proteins, including ferritin, catalase, superoxide dismutase, bovine serum albumin (BSA), and ovalbumin, have been modified by amidation to increase their interaction with negatively charged tissues . Moreover, cationic BSA was found to form polyplexes with plasmid DNA that allowed transfection of A549 human lung epithelial cells in vitro .…”

Section: Engineering Supercharged Folded Proteinsmentioning

confidence: 99%

Supercharged Proteins and Polypeptides

Malessa

Boersma

et al. 2020

Advanced Materials

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Electrostatic interactions play a vital role in nature. Biomacromolecules such as proteins are orchestrated by electrostatics, among other intermolecular forces, to assemble and organize biochemistry. Natural proteins with a high net charge exist in a folded state or are unstructured and can be an inspiration for scientists to artificially supercharge other protein entities. Recent findings show that supercharging proteins allows for control of their properties such as temperature resistance and catalytic activity. One elegant method to transfer the favorable properties of supercharged proteins to other proteins is the fabrication of fusions. Genetically engineered, supercharged unstructured polypeptides (SUPs) are just one promising fusion tool. SUPs can also be complexed with artificial entities to yield thermotropic and lyotropic liquid crystals and liquids. These architectures represent novel bulk materials that are sensitive to external stimuli. Interestingly, SUPs undergo fluid–fluid phase separation to form coacervates. These coacervates can even be directly generated in living cells or can be combined with dissipative fiber assemblies that induce life‐like features. Supercharged proteins and SUPs are developed into exciting classes of materials. Their synthesis, structures, and properties are summarized. Moreover, potential applications are highlighted and challenges are discussed.

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Section: Engineering Supercharged Folded Proteinsmentioning

confidence: 99%

Supercharged Proteins and Polypeptides

Malessa

Boersma

et al. 2020

Advanced Materials

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“…Biocatalyst immobilization, which may also improve stability and simplify product separation [20,21], can be achieved on the inner surface of the microchannels [21,41,[54][55][56][57][58], in microscale reactors with monolithic structures [59][60][61] or nanostructured material within the microspace [22,23], entrapped in the bulk space within porous structures [32,[62][63][64][65][66][67][68] or with the assistance of a magnetic field [69] (Table 2). For example, a comparison of various immobilization methods and supports for threonine aldolases showed a sufficient loading performance under best performance assumptions only when high-value products like pharmaceuticals were considered [23].…”

Section: Biocatalyst Configurationmentioning

confidence: 99%

Microscale technology and biocatalytic processes: opportunities and challenges for synthesis

Wohlgemuth¹,

Plazl

Žnidaršič–Plazl

et al. 2015

Trends in Biotechnology

181

151

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“…24 Additionally, biofilms formed by the immobilization of cBSA showed outstanding compatibility in the fixation of lipid vesicles and whole cells. 25,26 These cells remain viable and catalyze the enantio-selective reduction of ethyl acetoacetate to R-(˗)ethyl-hydroxybutyrate in a microchannel reactor . 26 On the other hand, HSA modified by second generation PAMAM dendrons (DHSA) has a unique implication in its design.…”

Section: Tailoring Hybrid Globular Proteins As Macromolecular Solutiomentioning

confidence: 99%

Programming Supramolecular Biohybrids as Precision Therapeutics

Kuan

et al. 2014

Acc. Chem. Res.

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CONSPECTUS: Chemical programming of macromolecular structures to instill a set of defined chemical properties designed to behave in a sequential and precise manner is a characteristic vision for creating next generation nanomaterials. In this context, biopolymers such as proteins and nucleic acids provide an attractive platform for the integration of complex chemical design due to their sequence specificity and geometric definition, which allows accurate translation of chemical functionalities to biological activity. Coupled with the advent of amino acid specific modification techniques, "programmable" areas of a protein chain become exclusively available for any synthetic customization. We envision that chemically reprogrammed hybrid proteins will bridge the vital link to overcome the limitations of synthetic and biological materials, providing a unique strategy for tailoring precision therapeutics. In this Account, we present our work toward the chemical design of protein- derived hybrid polymers and their supramolecular responsiveness, while summarizing their impact and the advancement in biomedicine. Proteins, in their native form, represent the central framework of all biological processes and are an unrivaled class of macromolecular drugs with immense specificity. Nonetheless, the route of administration of protein therapeutics is often vastly different from Nature's biosynthesis. Therefore, it is imperative to chemically reprogram these biopolymers to direct their entry and activity toward the designated target. As a consequence of the innate structural regularity of proteins, we show that supramolecular interactions facilitated by stimulus responsive chemistry can be intricately designed as a powerful tool to customize their functions, stability, activity profiles, and transportation capabilities. From another perspective, a protein in its denatured, unfolded form serves as a monodispersed, biodegradable polymer scaffold decorated with functional side chains available for grafting with molecules of interest. Additionally, we are equipped with analytical tools to map the fingerprint of the protein chain, directly elucidating the structure at the molecular level. Contrary to conventional polymers, these biopolymers facilitate a more systematic avenue to investigate engineered macromolecules, with greater detail and accuracy. In this regard, we focus on denaturing serum albumin, an abundant blood protein, and exploit its peptidic array of functionalities to program supramolecular architectures for bioimaging, drug and gene delivery. Ultimately, we seek to assimilate the evolutionary advantage of these protein based biopolymers with the limitless versatility of synthetic chemistry to merge the best of both worlds.

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cBSA-147 for the preparation of bacterial biofilms in a microchannel reactor

Cited by 11 publications

References 23 publications

Supercharged Proteins and Polypeptides

Supercharged Proteins and Polypeptides

Microscale technology and biocatalytic processes: opportunities and challenges for synthesis

Programming Supramolecular Biohybrids as Precision Therapeutics

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