By a News Reporter-Staff News Editor at Life Science Weekly -- Researchers detail new data in Peptides and Proteins. According to news reporting originating in Bologna, Italy, by NewsRx journalists, research stated, "Integrating carbon nanotubes (CNTs) with biological systems to form hybrid functional assemblies is an innovative research area with great promise for medical, nanotechnology, and materials science applications. The specifics of molecular recognition and catalytic activity of proteins combined with the mechanical and electronic properties of CNTs provides opportunities for physicists, chemists, biologists, and materials scientists to understand and develop new nanomachines, sensors, or any of a number of other molecular assemblies."
The news reporters obtained a quote from the research from the University of Bologna, "Researchers know relatively little about the structure, function, and spatial orientation of proteins non-covalently adsorbed on CNTs, yet because the interaction of CNTs with proteins depends strongly on the tridimensional structure of the proteins, many of these questions can be answered in simple terms. In this Account, we describe recent research investigating the properties of CNT/protein hybrids. Proteins act to solvate CNTs and may sort them according to diameter or chirality. In turn, CNTs can support and immobilize enzymes, creating functional materials. Additional applications include proteins that assemble ordered hierarchical objects containing CNTs, and CNTs that act as protein carriers for vaccines, for example. Protein/CNT hybrids can form bioscaffolds and can serve as therapeutic and imaging materials. Proteins can detect CNTs or coat them to make them biocompatible. One of the more challenging applications for protein/CNT hybrids is to make CNT substrates for cell growth and neural interfacing applications. The challenge arises from the structures' interactions with living cells, which poses questions surrounding the (nano)toxicology of CNTs and whether and how CNTs can detect biological processes or sense them as they occur. The surface chemistry of CNTs and proteins, including interactions such as pi-pi stacking interactions, hydrophobic interactions, surfactant-like interactions, and charge-pi interactions, governs the wealth of structures, processes, and functions that appear when such different types of molecules interact. Each residue stars in one of two main roles, and understanding which residues are best suited for which type of interaction can lead to the design of new hybrids. Non locally, the peptide or protein primary, secondary, and tertiary structures govern the binding of proteins by CNTs. The conjugation of proteins with CNTs presents some serious difficulties both experimentally and culturally (such as bridging the 'jargon barrier' across disciplines). The intersection of these fields lies between communities characterized by distinctly different approaches and methodologies."
According to the news reporters, the research concluded: "However, the examples of this Account illustrate that when this barrier is overcome, the exploitation of hybrid CNT-protein systems offers great potential."
For more information on this research see: The Devil and Holy Water: Protein and Carbon Nanotube Hybrids. Accounts of Chemical Research, 2013;46(11):2454-2463. 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)
Our news correspondents report that additional information may be obtained by contacting M. Calvaresi, University of Bologna, Dipartimento Chim G Ciamician, I-40126 Bologna, Italy (see also Peptides and Proteins).
Keywords for this news article include: Italy, Europe, Bologna, Fullerenes, Amino Acids, Carbon Nanotubes, Peptides and Proteins
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