Over the past decade, synthetic biology has emerged as an engineering discipline for biological systems. Compared with other substrates, biology poses a unique set of engineering challenges resulting from an incomplete understanding of natural biological systems and tools for manipulating them. To address these challenges, synthetic biology is advancing from developing proof-of-concept designs to focusing on core platforms for rational and high-throughput biological engineering. These platforms span the entire biological design cycle, including DNA construction, parts libraries, computational design tools, and interfaces for manipulating and probing synthetic circuits. The development of these enabling technologies requires an engineering mindset to be applied to biology, with an emphasis on generalizable techniques in addition to application-specific designs. This review aims to discuss the progress and challenges in synthetic biology and to illustrate areas where synthetic biology may impact biomedical engineering and human health.
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http://dx.doi.org/10.1146/annurev-bioeng-071811-150118 | DOI Listing |
BMC Plant Biol
January 2025
Research Institute of Biology and Agriculture, School of Chemistry and Biological Engineering, Shunde Innovation School, Zhongzhi International Institute of Agricultural Biosciences, University of Science and Technology Beijing, Beijing, 100083, China.
Background: Anthocyanin is an important class of water-soluble pigments that are widely distributed in various tissues of plants, and it not only facilitates diverse color changes but also plays important roles in various biological processes. Maize silk, serving as an important reproductive organ and displaying a diverse range of colors, plays an indispensable role in biotic resistance through its possession of anthocyanin. However, the copy numbers, characteristics, and expression patterns of genes involved in maize anthocyanin biosynthesis are not fully understood.
View Article and Find Full Text PDFNat Struct Mol Biol
January 2025
Department of Biochemistry, Duke University School of Medicine, Durham, NC, USA.
Transient receptor potential channel subfamily M member 3 (TRPM3) is a Ca-permeable cation channel activated by the neurosteroid pregnenolone sulfate (PregS) or heat, serving as a nociceptor in the peripheral sensory system. Recent discoveries of autosomal dominant neurodevelopmental disorders caused by gain-of-function mutations in TRPM3 highlight its role in the central nervous system. Notably, the TRPM3 inhibitor primidone, an anticonvulsant, has proven effective in treating patients with TRPM3-linked neurological disorders and in mouse models of thermal nociception.
View Article and Find Full Text PDFNat Rev Chem
January 2025
Department of Chemistry & Biochemistry, University of California Santa Barbara, Santa Barbara, CA, USA.
Catechol-functionalized proteins in mussel holdfasts are essential for underwater adhesion and cohesion and have inspired countless synthetic polymeric materials and devices. However, as catechols are prone to oxidation, long-term performance and stability of these inventions awaits effective antioxidation strategies. In mussels, catechol-mediated interactions are stabilized by 'built-in' homeostatic redox reservoirs that restore catechols oxidized to quinones.
View Article and Find Full Text PDFNat Commun
January 2025
Institute of Marine Science and Technology, Shandong University, Qingdao, China.
Lignin, as the abundant carbon polymer, is essential for carbon cycle and biorefinery. Microorganisms interact to form communities for lignin biodegradation, yet it is a challenge to understand such complex interactions. Here, we develop a coastal lignin-degrading bacterial consortium (LD), through "top-down" enrichment.
View Article and Find Full Text PDFNat Commun
January 2025
Institute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montréal, QC, H3T 1J4, Canada.
Intense research on founding members of the RAS superfamily has defined our understanding of these critical signalling proteins, leading to the premise that small GTPases function as molecular switches dependent on differential nucleotide loading. The closest homologs of H/K/NRAS are the three-member RRAS family, and interest in the MRAS GTPase as a regulator of MAPK activity has recently intensified. We show here that MRAS does not function as a classical switch and is unable to exchange GDP-to-GTP in solution or when tethered to a lipid bilayer.
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