Manu Platt talks about the new NIH Center for Biomedical Engineering Technology Acceleration.

The National Institute of Biomedical Imaging and Bioengineering has established a new Center for Biomedical Engineering Technology Acceleration, dedicated to applying engineering principles to biomedical discovery and therapeutics. We talk to the Center's Director Manu Platt about their plans and the focus on diversity, equity, inclusion and accessibility.

Nebulized lipid nanoparticles.

An article in reports an in vivo workflow for the design of lipid nanoparticles to efficiently deliver mRNA to the lungs via nebulization.

From lipids to lipid nanoparticles to mRNA vaccines.

Lipid nanoparticles are essential to mRNA vaccines. The groundwork for lipid-based drug delivery systems was laid more than 40 years ago in the lab of Pieter Cullis, Professor at the University of British Columbia. talks to Pieter Cullis about the history and future of lipid nanoparticle-nucleic acid drugs.

Artificially intelligent nanopore for rapid SARS-CoV-2 testing.

An article in reports a method for the rapid detection of SARS-CoV-2 in saliva samples using nanopores and a machine learning algorithm.

Organ chips, organoids and the animal testing conundrum.

speaks to Donald Ingber, Founding Director of the Wyss Institute for Biologically Inspired Engineering at Harvard University, about the animal testing conundrum and the importance of human-relevant models in biomedical research.

Nanobiotechnology with S-layer proteins as building blocks.

One of the key challenges in nanobiotechnology is the utilization of self- assembly systems, wherein molecules spontaneously associate into reproducible aggregates and supramolecular structures. In this contribution, we describe the basic principles of crystalline bacterial surface layers (S-layers) and their use as patterning elements. The broad application potential of S-layers in nanobiotechnology is based on the specific intrinsic features of the monomolecular arrays composed of identical protein or glycoprotein subunits.

Single-molecule force spectroscopy reveals the individual mechanical unfolding pathways of a surface layer protein.

Surface layers (S-layers) represent an almost universal feature of archaeal cell envelopes and are probably the most abundant bacterial cell proteins. S-layers are monomolecular crystalline structures of single protein or glycoprotein monomers that completely cover the cell surface during all stages of the cell growth cycle, thereby performing their intrinsic function under a constant intra- and intermolecular mechanical stress. In gram-positive bacteria, the individual S-layer proteins are anchored by a specific binding mechanism to polysaccharides (secondary cell wall polymers) that are linked to the underlying peptidoglycan layer.

Monte Carlo study of the molecular mechanisms of surface-layer protein self-assembly.

The molecular mechanisms guiding the self-assembly of proteins into functional or pathogenic large-scale structures can be only understood by studying the correlation between the structural details of the monomer and the eventual mesoscopic morphologies. Among the myriad structural details of protein monomers and their manifestations in the self-assembled morphologies, we seek to identify the most crucial set of structural features necessary for the spontaneous selection of desired morphologies. Using a combination of the structural information and a Monte Carlo method with a coarse-grained model, we have studied the functional protein self-assembly into S(surface)-layers, which constitute the crystallized outer most cell envelope of a great variety of bacterial cells.

Atomistic structure of monomolecular surface layer self-assemblies: toward functionalized nanostructures.

The concept of self-assembly is one of the most promising strategies for the creation of defined nanostructures and therefore became an essential part of nanotechnology for the controlled bottom-up design of nanoscale structures. Surface layers (S-layers), which represent the cell envelope of a great variety of prokaryotic cells, show outstanding self-assembly features in vitro and have been successfully used as the basic matrix for molecular construction kits. Here we present the three-dimensional structure of an S-layer lattice based on tetrameric unit cells, which will help to facilitate the directed binding of various molecules on the S-layer lattice, thereby creating functional nanoarrays for applications in nanobiotechnology.

Surface layer protein characterization by small angle x-ray scattering and a fractal mean force concept: from protein structure to nanodisk assemblies.

Surface layers (S-layers) are the most commonly observed cell surface structure of prokaryotic organisms. They are made up of proteins that spontaneously self-assemble into functional crystalline lattices in solution, on various solid surfaces, and interfaces. While classical experimental techniques failed to recover a complete structural model of an unmodified S-layer protein, small angle x-ray scattering (SAXS) provides an opportunity to study the structure of S-layer monomers in solution and of self-assembled two-dimensional sheets.