We demonstrate the additive manufacturing of complex three-dimensional (3D) biological structures using soft protein and polysaccharide hydrogels that are challenging or impossible to create using traditional fabrication approaches. These structures are built by embedding the printed hydrogel within a secondary hydrogel that serves as a temporary, thermoreversible, and biocompatible support. This process, termed freeform reversible embedding of suspended hydrogels, enables 3D printing of hydrated materials with an elastic modulus <500 kPa including alginate, collagen, and fibrin. Computer-aided design models of 3D optical, computed tomography, and magnetic resonance imaging data were 3D printed at a resolution of ~200 μm and at low cost by leveraging open-source hardware and software tools. Proof-of-concept structures based on femurs, branched coronary arteries, trabeculated embryonic hearts, and human brains were mechanically robust and recreated complex 3D internal and external anatomical architectures.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4646826PMC
http://dx.doi.org/10.1126/sciadv.1500758DOI Listing

Publication Analysis

Top Keywords

biological structures
8
freeform reversible
8
reversible embedding
8
embedding suspended
8
suspended hydrogels
8
three-dimensional printing
4
printing complex
4
complex biological
4
structures freeform
4
hydrogels demonstrate
4

Similar Publications

Fully Atomistic Molecular Dynamics Simulation of Ice Nucleation Near an Antifreeze Protein.

J Am Chem Soc

January 2025

Department of Materials Science and Engineering, City University of Hong Kong, Hong Kong, Kowloon 999077, China.

Heterogeneous ice nucleation is a widespread phenomenon in nature. Despite extensive research on ice nucleation near biological antifreeze proteins, a probe for ice nucleation and growth processes at the atomic level is still lacking. Herein, we present simulation evidence of the heterogeneous ice nucleation process on the ice-binding surface (IBS) of the antifreeze protein (TmAFP).

View Article and Find Full Text PDF

Eukaryotic Initiation Factor 4 (eIF4) is a group of factors that activates mRNA for translation and recruit 43S preinitiation complex (PIC) to the mRNA 5' end, forming the 48S PIC. The eIF4 factors include mRNA 5' cap-binding protein eIF4E, ATP-dependent RNA helicase eIF4A, and scaffold protein eIF4G, which anchors eIF4A and eIF4E. Another eIF4 factor, eIF4B, stimulates the RNA helicase activity of eIF4A and facilitates mRNA recruitment.

View Article and Find Full Text PDF

RNA G-quadruplexes (rG4s), the four-stranded structures formed by guanine-rich RNA sequences, are recognized by regions in RNA-binding proteins (RBPs) that are enriched in arginine-glycine repeats (RGG motifs). Importantly, arginine and glycine are encoded by guanine-rich codons, suggesting that some RGG motifs may both be encoded by and interact with rG4s in autogenous messenger RNAs (mRNAs). By analyzing transcriptome-wide rG4 datasets, we show that hundreds of RGG motifs in humans are at least partly encoded by rG4s, with an increased incidence for longer RGG motifs (~10 or more residues).

View Article and Find Full Text PDF

Many proteins form paralogous multimers-molecular complexes in which evolutionarily related proteins are arranged into specific quaternary structures. Little is known about the mechanisms by which they acquired their stoichiometry (the number of total subunits in the complex) and heterospecificity (the preference of subunits for their paralogs rather than other copies of the same protein). Here, we use ancestral protein reconstruction and biochemical experiments to study historical increases in stoichiometry and specificity during the evolution of vertebrate hemoglobin (Hb), an αβ heterotetramer that evolved from a homodimeric ancestor after a gene duplication.

View Article and Find Full Text PDF

Metabolic activity controls the emergence of coherent flows in microbial suspensions.

Proc Natl Acad Sci U S A

January 2025

Experimental Physics V, Department of Physics, University of Bayreuth, D-95447 Bayreuth, Germany.

Photosynthetic microbes have evolved and successfully adapted to the ever-changing environmental conditions in complex microhabitats throughout almost all ecosystems on Earth. In the absence of light, they can sustain their biological functionalities through aerobic respiration, and even in anoxic conditions through anaerobic metabolic activity. For a suspension of photosynthetic microbes in an anaerobic environment, individual cellular motility is directly controlled by its photosynthetic activity, i.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!