An overview of the wide range of nanoreactors that have been constructed from synthetic and biological building blocks using both covalent and noncovalent approaches is given. Focus is on self-assembled systems, varying in size from a few nanometers to tens of micrometers. The review is divided into several sections that cover the development of tailor-made nanoreactors, starting from small organic molecular containers expanding to large compartment-containing assemblies. First, the construction of capsules from low molecular weight compounds by means of covalent synthesis and self-assembly by highly directive and pre-designed interactions is discussed. Second, nanocapsules based on micellar and vesicular assemblies that are built up frow low molecular weight molecules are described. Finally, the construction of nanoreactors from macromolecular building blocks, as well as recent developments in the use of viruses as nanocontainers and reactors are outlined.

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Self-Assembled Nanoreactors

Genomes of complex organisms encode an abundance and diversity of long noncoding RNAs (lncRNAs) that are expressed throughout the cell and fulfill a wide variety of regulatory roles at almost every stage of gene expression. These roles, which encompass sensory, guiding, scaffolding and allosteric capacities, derive from folded modular domains in lncRNAs. In this diverse functional repertoire, we focus on the well-characterized ability for lncRNAs to function as epigenetic modulators. Many lncRNAs bind to chromatin-modifying proteins and recruit their catalytic activity to specific sites in the genome, thereby modulating chromatin states and impacting gene expression. Considering this regulatory potential in combination with the abundance of lncRNAs suggests that lncRNAs may be part of a broad epigenetic regulatory network.

Structure and function of long noncoding RNAs in epigenetic regulation

Small Angle Scattering of X-Rays

A review of lignocellulose bioconversion using enzymatic hydrolysis and synergistic cooperation between enzymes--factors affecting enzymes, conversion and synergy.

Not all adaptive immune systems use the immunoglobulin fold as the basis for specific recognition molecules: sea lampreys, for example, have evolved an adaptive immune system that is based on leucine-rich repeat proteins. Additionally, many other proteins, not necessarily involved in adaptive immunity, mediate specific high-affinity interactions. Such alternatives to immunoglobulins represent attractive starting points for the design of novel binding molecules for research and clinical applications. Indeed, through progress and increased experience in library design and selection technologies, gained not least from working with synthetic antibody libraries, researchers have now exploited many of these novel scaffolds as tailor-made affinity reagents. Significant progress has been made not only in the basic science of generating specific binding molecules, but also in applications of the selected binders in laboratory procedures, proteomics, diagnostics and therapy. Challenges ahead include identifying applications where these novel proteins can not only be an alternative, but can enable approaches so far deemed technically impossible, and delineate those therapeutic applications commensurate with the molecular properties of the respective proteins.

Engineering novel binding proteins from nonimmunoglobulin domains

Synthesis of functional protein in liposome.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2004.09.046

Expression of a cascading genetic network within liposomes

We describe a new method of random mutagenesis that employs the addition of peptide tails with random sequences to the C–terminal of enzyme molecules. A mutant population of catalase I from Bacillus stearothermophilus prepared by this method has a diversity in thermostability and enzyme activity equal to that obtained after random point mutagenesis. When a triple mutant of catalase I (I108T/D130N/I222T)—the thermostability of which is much lower than that of the wild type—was subjected to random elongation mutagenesis, we generated a mutant population containing only mutants with higher thermostability than the triple mutant. Some had an even higher stability than the wild–type enzyme, whose thermostability is considered to be optimized. These results indicate that peptide addition expands the protein sequence space resulting in a new fitness landscape. The enzyme can then move along the routes of the new landscape until it reaches a new optimum. The combination of random elongation mutagenesis with random point mutagenesis should be a useful approach to the in vitro evolution of proteins with new properties.

Evolutionary molecular engineering by random elongation mutagenesis

http://faperta.ugm.ac.id/download/publikasi_dosen/irfan_dp/pdf/05-1996-Solubility%20of%20artificial%20proteins%20with%20random%20sequences.pdf

Solubility of artificial proteins with random sequences

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2897%2901552-4

Yasufumi Shima

Papers

Synthesis of functional protein in liposome.

Expression of a cascading genetic network within liposomes

Evolutionary molecular engineering by random elongation mutagenesis

Solubility of artificial proteins with random sequences

Characterization of soluble artificial proteins with random sequences