59 papers
Synthetic biology is like engineering for life, where scientists design and build new biological parts or rewire existing ones to solve real-world problems. Instead of just studying how nature works, this field asks what we can create, from bacteria that produce biofuels to smart materials that heal themselves. It sits at the exciting intersection of biology, engineering, and computer science, turning the code of life into something we can read, edit, and program.
At Gist.Science, we bring you the very latest discoveries in this rapidly evolving space directly from bioRxiv. We process every new preprint in this category as soon as it appears, offering both plain-language explanations for the curious mind and detailed technical summaries for researchers. This ensures you never miss a breakthrough, regardless of your background or how deep you want to dive into the science.
Below are the newest preprints in synthetic biology, carefully curated and summarized just for you.
This paper proposes a novel, function-aware screening framework for AI-enabled protein design tools that targets potentially harmful human proteoforms using the ESM-C language model, offering a balanced approach to mitigate biosecurity risks while preserving legitimate scientific research.
This study demonstrates that mRNA-DNA hybrid origami can simultaneously enhance stability and enable efficient translation by strategically exposing the first 35 nucleotides of the coding region while allowing ribosomes to displace DNA staples during elongation, with N1-methylpseudouridine chemistry providing the highest output despite increased sensitivity to overhang length.
This study introduces ActiveDROPS to demonstrate that specific modular configurations of kinesin motor domains dictate distinct classes of microtubule dynamics, enabling the rational engineering of chimeric motors to precisely control the velocity and duration of cytoskeletal flows.
This study demonstrates that engineering plants to biosynthesize the non-canonical amino acid O-methyl-L-tyrosine enables plant hosts to programmably control gene expression and activity in associated soil bacteria, establishing a new platform for precision agricultural biotechnology.
This paper demonstrates that diversity-generating retroelements (DGRs) can be engineered in *Escherichia coli* and coupled with horizontal gene transfer to create a simple, programmable system for the continuous, iterative, and position-specific mutagenesis of target genes, enabling the rapid evolution of proteins such as pyrrolysyl-tRNA synthetase for biotechnological applications.
This study presents a clinically compatible, reversible strategy for controlling CAR T cell function using human estrogen receptor-based degron domains that enable precise pharmacological ON-switch activation via 4-hydroxytamoxifen and OFF-switch degradation via the FDA-approved PROTAC ARV-471, thereby enhancing the safety and precision of cellular immunotherapies.
This study demonstrates that inserting a bulky, inert protein domain at residue L68 of the TadA8e adenine base editor creates a precise variant with a narrowed editing window, reduced off-target effects, and built-in fluorescence tracking capabilities.
This study establishes blue-light-inducible optogenetic switches in the corn fungal pathogen *Ustilago maydis* to achieve precise, reversible, and dynamic control over gene expression, thereby enabling the manipulation of cell morphology, filamentous invasion, and tumor formation for advanced research into pathogen-host interactions and biotechnological applications.
This paper presents a scalable, modular, and automated robotic pipeline using the CyBio FeliX platform and SPRI-based magnetic bead technology to efficiently purify high-quality plasmid DNA, successfully enabling the construction and validation of a 528-plasmid lentiviral library for mammalian cell lineage tracing.
By grafting the anticodon-binding domain of lysyl-tRNA synthetase onto the protein ligase EpmA, researchers engineered a chimeric enzyme (chEpmA) that successfully reprograms a protein ligase into a versatile aminoacyl-tRNA synthetase capable of charging tRNAs with diverse non-canonical substrates, including {beta}-amino acids and various post-translational modifications, to expand the genetic code.