By a News Reporter-Staff News Editor at Life Science Weekly -- Fresh data on Proteomics are presented in a new report. According to news reporting originating from La Jolla, California, by NewsRx correspondents, research stated, "The lipid bilayer membranes are Natures dynamic structural motifs that individualize cells and keep ions, proteins, biopolymers and metabolites confined in the appropriate location. The compartmentalization and isolation of these molecules from the external media facilitate the sophisticated functions and connections between the different biological processes accomplished by living organisms."
Our news editors obtained a quote from the research from Scripps Research Institute, "However, cells require assistance from minimal energy shortcuts for the transport of molecules across membranes so that they can interact with the exterior and regulate their internal environments. Ion channels and pores stand out from all other possible transport mechanisms due to their high selectivity and efficiency in discriminating and transporting ions or molecules across membrane barriers. Nevertheless, the complexity of these smart 'membrane holes' has driven researchers to develop simpler artificial structures with comparable performance to the natural systems. As a broad range of supramolecular interactions have emerged as efficient tools for the rational design and preparation of stable 3D superstructures, these results have stimulated the creativity of chemists to design synthetic mimics of natural active macromolecules and even to develop artificial structures with functions and properties. In this Account, we highlight results from our laboratories on the construction of artificial ion channel models that exploit the self-assembly of conformationally flat cyclic peptides (CPs) into supramolecular nanotubes. Because of the straightforward synthesis of the cyclic peptide monomers and the complete control over the internal diameter and external surface properties of the resulting hollow tubular suprastructure, CPs are the optimal candidates for the fabrication of ion channels. The ion channel activity and selective transport of small molecules by these structures are examples of the great potential that cyclic peptide nanotubes show for the construction of functional artificial transmembrane transporters."
According to the news editors, the research concluded: "Our experience to date suggests that the next steps for achieving conceptual devices with better performance and selectivity will derive from the topological control over cyclic peptide assembly and the functionalization of the lumen."
For more information on this research see: Ion Channel Models Based on Self-Assembling Cyclic Peptide Nanotubes. Accounts of Chemical Research, 2013;46(12):2955-2965. Accounts of Chemical Research can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Accounts of Chemical Research - www.pubs.acs.org/journal/achre4)
The news editors report that additional information may be obtained by contacting J. Montenegro, Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037, United States. Additional authors for this research include M.R. Ghadiri and J.R. Granja (see also Proteomics).
Keywords for this news article include: La Jolla, California, Proteomics, Ion Channels, United States, Nanotechnology, Supramolecular, Cyclic Peptides, Peptide Nanotubes, Emerging Technologies, Membrane Glycoproteins, North and Central America, Membrane Transport Proteins
Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC