Since the 1970s technological advancements in the fields of synthetic biology and metabolic engineering have led to a dramatic reduction in both time and cost required for generating genomic mutations in a variety of organisms. The union of genomic editing machinery, DNA inkjet printers, and bioinformatics algorithms allows engineers to design a library of thousands of unique oligos as well as build and test these designs on a ∼2 months time-scale and at a cost of roughly ∼0.3 cents per base pair. The implications of these capabilities for a variety of fields are far-reaching, with potential impacts in defense, agricultural, human health, and environmental research. The explosion of synthetic biology applications over the past two decades have led many to draw parallels between biological engineering and the computer sciences. In this review, we highlight some important parallels between these fields and emphasize the importance of engineering design strategies.
This work was done by members of the lab, The NanoBiotechnology Research Group, as an effort to generally explain some of the research proyects currently ...
Protein-protein interactions are fundamental to many biological processes. Yet the weak and transient non-covalent bonds that characterize most protein-protein interactions found in nature impose limits on many bioengineering experiments. Here a new class of genetically encodable peptide-protein pairs—isopeptag-N/pilin-N, isopeptag/pilin-C, and SpyTag-SpyCatcher—that interact via autocatalytic intermolecular isopeptide bond formation is described. Reactions between peptide-protein pairs are specific, robust, orthogonal, and able to proceed under most biologically relevant conditions both in vitro and in vivo. As fusion constructs they provide a handle on molecules of interest, both organic and inorganic, that can be grasped with an iron grip. Such stable interactions provide robust post-translational control over biological processes, and open new opportunities in synthetic biology for engineering programmable and self-assembling protein nanoarchitectures.
The next time you look in a mirror, think about this: In many ways you're more microbe than human. There are 10 times more cells from microorganisms like bac...
Cell-free protein synthesis is a promising tool to take biotechnology outside of the cell. A cell-free approach provides distinct advantages over in vivo systems including open access to the reaction environment and direct control over all chemical components for facile optimization and synthetic biology integration. Promising applications of cell-free systems include portable diagnostics, biotherapeutics expression, rational protein engineering, and biocatalyst production. The highest yielding and most economical cell-free systems use an extract composed of the soluble component of lysed Escherichia coli. Although E. coli lysis can be highly efficient (>99.999%), one persistent challenge is that the extract remains contaminated with up to millions of cells per mL. In this work, we examine the potential of multiple decontamination strategies to further reduce or elimiate bacteria in cell-free systems. Two strategies, sterile filtration and lyophilization, effectively eliminate contaminating cells while maintaining the systems' protein synthesis capabilities. Lyophilization provides the additional benefit of long-term stability at storage above freezing. Technologies for personalized, portable medicine and diagnostics can be expanded based on these foundational sterilized and completely "cell-free" systems. This article is protected by copyright. All rights reserved.
DNA assembly is a key part of constructing gene expression systems and even whole chromosomes. In the past decade, a plethora of powerful new DNA assembly methods - including Gibson Assembly, Golden Gate and ligase cycling reaction (LCR) - have been developed. In this Innovation article, we discuss these methods as well as standards such as the modular cloning (MoClo) system, GoldenBraid, modular overlap-directed assembly with linkers (MODAL) and PaperClip, which have been developed to facilitate a streamlined assembly workflow, to aid the exchange of material between research groups and to create modular reusable DNA parts.
The Escapist Synthetic Biology Could Let Us Recycle Human Waste For Space Travel The Escapist One day, astronauts might recycle urine and carbon dioxide into highly necessary food and medicines for space missions.
GenoCAD, a computer-assisted design environment for synthetic biology developed at Virginia Tech, has transitioned to GenoFAB LLC to engage new users and create new opportunities for innovation.
Beer and Biosensors: join us for a fun and informative evening exploring sensors both genetic and electronic.
• "A (very) brief introduction to sensors"
• Beer Sensors (hands-on activity for everyone)
• "Sensors, beer and brewing: what do the results mean?"
Paul Grant and James Godman, University of Cambridge and Hop Back Brewery
Discussion throug...
Beer and Biosensors: join us for a fun and informative evening exploring sensors both genetic and electronic. • "A (very) brief introduction to sensors" • "Designing and prototyping gen
The world's first functioning organism with an expanded DNA alphabet has now met another milestone in artificial life: making proteins that don't exist in nature.
The organism, a bacterium created by scientists at The Scripps Research Institute, incorporates two synthetic DNA letters, called X and Y, along with the four natural ones, A, T, C and G. A team led by Floyd Romesberg published a study last year demonstrating that the organism, an engineered strain of E. coli, can function and replicate with the synthetic DNA.
Synthorx, a biotech startup that licensed the technology from Scripps, has now used the bacterium to produce proteins incorporating artificial amino acids, the building blocks of proteins. These are placed at precisely specified intervals along the protein sequence, obeying the code of the expanded DNA alphabet.
Synthetic biology is a recent scientific approach towards engineering biological systems from both pre-existing and novel parts. The aim is to introduce computational aided design approach in biology leading to rapid delivery of useful applications. Though the term reprogramming has been frequently used in the synthetic biology community, currently the technological sophistication only allows for a probabilistic approach instead of a precise engineering approach. Recently, several human health applications have emerged that suggest increased usage of synthetic biology approach in developing novel drugs. This mini review discusses recent translational developments in the field and tries to identify some of the upcoming future developments.
Extracellular electron transfer pathways allow certain bacteria to transfer energy between intracellular chemical energy stores and extracellular solids through redox reactions. Microorganisms containing these pathways, exoelectrogens, are a critical part of microbial electrochemical technologies that aim to impact applications in bioenergy, biosensing, and biocomputing. However, there are not yet any examples of economically viable microbial electrochemical technologies due to the limitations of naturally-occurring exoelectrogens. Here we first briefly summarize recent discoveries in understanding extracellular electron transfer pathways, then review in-depth the creation of customized and novel exoelectrogens for biotechnological applications. We analyze engineering efforts to increase current production in native exoelectrogens, which reveals that modulating certain processes within extracellular electron transfer are more effective than others. We also review efforts to create new exoelectrogens and highlight common challenges in this work. Lastly, we summarize work utilizing engineered exoelectrogens for biotechnological applications and the key obstacles to their future development. Fueled by the development of genetic tools, these approaches will continue to expand and genetically modified organisms will continue to improve the outlook for microbial electrochemical technologies.
Protein-protein interactions (PPIs) are important targets for understanding fundamental biology and for the development of therapeutic agents. Based on different physicochemical properties, numerous pieces of software (e.g., POCKETQUERY, ANCHORQUERY and FTMap) have been reported to find pockets on protein surfaces and have applications in facilitating the design and discovery of small-molecular-weight compounds that bind to these pockets. Areas covered: The authors discuss a pocket-centric method of analyzing PPI interfaces, which prioritize their pockets for small-molecule drug discovery and the importance of multicomponent reaction chemistry as starting points for undruggable targets. The authors also provide their perspectives on the field. Expert opinion: Only the tight interplay of efficient computational methods capable of screening a large chemical space and fast synthetic chemistry will lead to progress in the rational design of PPI antagonists in the future. Early drug discovery platforms will also benefit from efficient rapid feedback loops from early clinical research back to molecular design and the medicinal chemistry bench.
“Many processes inside cells are controlled by protein–protein interactions and therefore developing new methods to regulate the assembly of protein structures could have a myriad of applications in synthetic biology. However, designing new proteins that selectively interact and that can assemble in vivo requires the design…”
The ability to quickly and reliably assemble DNA constructs is one of the key enabling technologies for synthetic biology. Here we define a new Biopart Assembly Standard for Idempotent Cloning (BASIC), which exploits the principle of orthogonal linker based DNA assembly to define a new physical standard for DNA parts. Further, we demonstrate a new robust method for assembly, based on type IIs restriction enzyme cleavage and ligation of oligonucleotides with single stranded overhangs that determine the assembly order. It allows for efficient, parallel assembly with great accuracy: 4 part assemblies achieved 93% accuracy with single antibiotic selection and 99.7% accuracy with double antibiotic selection, while 7 part assemblies achieved 90% accuracy with double antibiotic selection. The linkers themselves may also be used as composable parts for RBS tuning or the creation of fusion proteins. The standard has one forbidden restriction site and provides for an idempotent, single tier organization, allowing all parts and composite constructs to be maintained in the same format. This makes the BASIC standard conceptually simple at both the design and experimental levels.
To get content containing either thought or leadership enter:
To get content containing both thought and leadership enter:
To get content containing the expression thought leadership enter:
You can enter several keywords and you can refine them whenever you want. Our suggestion engine uses more signals but entering a few keywords here will rapidly give you great content to curate.
Your new post is loading...
Scoop.it!
