By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Proteins have been published. According to news reporting originating in Ulsan, South Korea, by NewsRx journalists, research stated, "A new dipyridyl ligand is encoded with 120° angularity between its coordination vectors by using a central pyridine carboxamide scaffold to orient two 4-(pyridin-4-ylethynyl)phenyl moieties. The N,N'-bis(4-(pyridin-4-ylethynyl)phenyl)pyridine-2,6-dicarboxamide ligand undergoes self-assembly with a diruthenium arene complex to furnish a [2 + 2] metallacycle with a wedge-like structure."
The news reporters obtained a quote from the research from the University of Ulsan, "The metallacycle binds to the enhanced green fluorescent protein (EGFP) variant of GFP, resulting in steady-state spectral changes in UV-Vis absorption and emission experiments. These studies indicate that the metallacycle induces conformation changes to the EGFP, disrupting the tripeptide chromophore. Furthermore, gel electrophoresis, circular dichroism and atomic force microscopy studies indicate that binding ultimately leads to aggregation of the protein. Computational investigations indicate a favorable interaction, predominantly between the metallacycle and the Arg168 residue of the EGFP. An interaction with Arg168 and related residues was previously observed for an emission-attenuating antibody, supporting that these interactions induce changes to the photophysical properties of EGFP by disrupting the tripeptidechromophore in a similar manner. Additionally, we have also described the quenching study of the reporter GFP protein in vivo by a new metal complex using reflected fluorescence microscopy."
According to the news reporters, the research concluded: "We anticipate that such metal complexes which can passively diffuse into the cells in vivo can serve as potential tools in molecular and drug targeting based biological studies."
For more information on this research see: A new arene-Ru based supramolecular coordination complex for efficient binding and selective sensing of green fluorescent protein. Dalton Transactions, 2014;43(16):6032-40. (Royal Society of Chemistry - www.rsc.org/; Dalton Transactions - pubs.rsc.org/en/journals/journalissues/dt)
Our news correspondents report that additional information may be obtained by contacting A. Mishra, Dept. of Chemistry, University of Ulsan, Ulsan 680-749, South Korea. Additional authors for this research include S. Ravikumar, Y.H. Song, N.S. Prabhu, H. Kim, S.H. Hong, S. Cheon, J. Noh and K.W Chi (see also Proteins).
Keywords for this news article include: Asia, Ulsan, South Korea, Nanotechnology, Supramolecular, Luminescent Proteins, Emerging Technologies, Green Fluorescent Proteins.
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