A set of Ru(ii) metallopeptides containing the dppz ligand has been synthesized using SPPS methods. Fluorescence titration studies show that those metallopeptides featuring an octaarginine tail display a large binding preference for DNA G-quadruplex structures over those lacking it, and also that the interplay between the octoarginine functionalization and the ancillary ligand in the complex has an essential role in the recognition process. Furthermore, the oligoarginine metallopeptides are also efficiently internalized, causing cell death with signs of apoptosis.
Die gemischten Hexahalogenokomplexe [OsClnX6–n]2−, X = Br, J; n = 1–5 einschließlich der für n = 2, 3, 4 existierenden Stereoisomerenpaare werden durch Ionenaustauschchromatographie an Diäthylaminoäthylcellulose (DEAE) mit verdünnten Mineralsäuren getrennt. Die spektrophotometrische Untersuchung ergibt, daß die früher durch stereospezifischen Ligandenaustausch mit anschließender ionophoretischer Isolierung erhaltenen cis‐ bzw. trans‐Komplexe nicht völlig rein sind.
We propose that peptides are highly versatile platforms for the precise design of supramolecular metal architectures, and particularly, for the controlled assembly of helicates. In this context, we show that the bacteriophage T4 Fibritin foldon (T4Ff) can been engineered on its N-terminus with metal-chelating 2,2′-bipyridine units that stereoselectively assemble in the presence of Fe(II) into parallel, three-stranded peptide helicates with preferred helical orientation. Modeling studies support the proposed self-assembly and the stability of the final helicate. Furthermore, we show that these designed mini-metalloproteins selectively recognize three-way DNA junctions over double-stranded DNA.
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