A hydrophobic disordered peptide spontaneously anchors a covalently bound RNA hairpin to giant lipidic vesicles.

The attraction of nucleic acids to lipidic compartments is the first step for carriers of potentially inheritable information to self-organise in functionalised synthetic cells. Confocal fluorescence imaging shows that a synthetic amphiphilic peptidyl RNA molecule spontaneously accumulates at the outer bilayer membranes of phospho- and glycolipidic giant vesicles. Cooperatively attractive interactions of -3.

Probing the leucyl/phenylalanyl tRNA protein transferase active site with tRNA substrate analogues.

Aminoacyl-tRNA protein transferases post-translationally conjugate an amino acid from an aminoacyl-tRNA onto the N-terminus of a target polypeptide. The eubacterial aminoacyl-tRNA protein transferase, L/F transferase, utilizes both leucyl-tRNA(Leu) and phenylalanyl-tRNA(Phe) as substrates. X-ray crystal structures with substrate analogues, the minimal substrate phenylalanyl adenosine (rA-Phe) and inhibitor puromycin, have been used to characterize tRNA recognition by L/F transferase.

The shortest synthetic route to puromycin analogues using a modified Robins approach.

We are reporting on the utility of commercial vinyl isocyanate for a practical synthetic route from adenosine to N(6)-bis-demethylpuromycin in seven steps and 65% overall yield. A clean one-pot conversion of 3'-bromo-2'-carbamoyl derivative 8 to 3'-amino-3'-deoxyadenosine derivative 10 is the main feature of this synthetic pathway. This synthesis is the shortest synthetic route toward 3'-(aminoacylamido)deoxyadenosines to date.

Intrinsic pKa values of 3'-N-α-l-aminoacyl-3'-aminodeoxyadenosines determined by pH dependent 1H NMR in H2O.

3'-(α-L-Aminoacylamido)deoxyadenosines are ribosomal A-site binders and mimic the nascent peptide accepting 3'-terminus of aminoacyl transfer RNA. Their α-amino groups exhibit intrinsic basicities in bulk water that differ by up to 1.8 pK(a) units.

Total synthesis of a xylo-Puromycin analog.

N(6)-bis-demethylated xylo-Puromycin analog 2 was synthesized in 56% over 6 steps from adenosine 3, involving a Mattocks bromo acetylation, a regio- and stereo-selective ribo-epoxide ring opening with sodium azide and an efficient Staudinger-Vilarrasa coupling reaction for which the conditions have been optimized.

Structural and functional prerequisites for ribosomal nascent peptide acceptors: attempts to decipher the nature of the ribosome's catalysis of peptide bond formation.

Aminoacyl ribonucleoside analogues that are capable of binding to the acceptor site of ribosomes and taking over the nascent peptide bear, if properly designed, the potential of antibiotic and cytostatic activity. Here we present a study on the intrinsic conformations of natural and synthetic peptide acceptors and the basicities of their peptide accepting amino groups. The conformations and thermodynamic parameters of several synthetic puromycin analogues have been elucidated through ab initio calculations as well as temperature and pH dependent (1)H NMR experiments.