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Biology subjects

Wee, J.

Publications and source records attributed to Wee, J..

2 recordsLinked to original sources

A proposed framework for evaluating meat alternatives

Concerns surrounding the environmental, economic, and ethical consequences of meat production and industrial agriculture have prompted substantial research and capital investment into the production of meat alternatives. Alternative meat production encompasses a variety of technological approaches including plant-based meats, cell-based or cultivated meats, meat alternatives relying on fungal protein sources, and hybrids thereof; each of which offers unique advantages and disadvantages and has been associated with a myriad of claims supporting it as the preferred alternative to animal-derived meats. As part of XPRIZE Foundations Feed the Next Billion competition, we developed a framework for evaluating meat alternatives by measuring their structural, nutritional, and organoleptic properties while also assessing safety and their purported environmental and economic benefits compared to animal-derived meats. The framework is technologically agnostic and can be used to evaluate meat alternatives of all types. The output of the framework enables a data-driven comparison to animal-derived meat and/or other alternative meats, allowing a range of stakeholders (e.g., food startups, investors, government) to assess technological readiness, competitive advantage, and impact potential. This framework can assist this nascent industry as it moves towards standardizing approaches to evaluating the quality, safety and proposed benefits of meat alternatives.

bioengineering↗

Multi-pass, single-molecule nanopore reading of long protein strands with single-amino acid sensitivity

The ability to sequence single protein molecules in their native, full-length form would enable a more comprehensive understanding of proteomic diversity. Current technologies, however, are limited in achieving this goal. Here, we establish a method for long-range, single-molecule reading of intact protein strands on a commercial nanopore sensor array. By using the ClpX unfoldase to ratchet proteins through a CsgG nanopore, we achieve single-amino acid level sensitivity, enabling sequencing of combinations of amino acid substitutions across long protein strands. For greater sequencing accuracy, we demonstrate the ability to reread individual protein molecules, spanning hundreds of amino acids in length, multiple times, and explore the potential for high accuracy protein barcode sequencing. Further, we develop a biophysical model that can simulate raw nanopore signals a priori, based on amino acid volume and charge, enhancing the interpretation of raw signal data. Finally, we apply these methods to examine intact, folded protein domains for complete end-to-end analysis. These results provide proof-of-concept for a platform that has the potential to identify and characterize full-length proteoforms at single-molecule resolution.

biophysics↗