Journal of Peptide Science

The replication of picornaviruses is primed by a small so-called VPg protein linked to a uridylyl residue. We report a general procedure to obtain such nucleoproteins employing a pre-uridylylated tyrosine building block in an on-line solid phase based approach.

Systematic SAR analyses were conducted to investigate the effects of altering PTH 1–11 peptide hydrophobicity on PTH receptor functional potency. Here, we report several novel PTH 1–11 peptidomimetics that show comparable or enhanced potency to stimulate G_s-signaling over β-arrestin recruitment as compared with such properties of PTH 1–34 and the Parent Peptide.

The β-sheet breakers – peptide inhibitors of amyloidogenesis: iAβ5 and newly designed iAβ6, containing two and three consecutive phenylalanine residues, respectively, acquired in MD simulations dominantly populated conformations with phenylalanine rings stacked. We postulate that stacking of aromatic rings facilitate anti-amyloidogenic properties of these peptides by targeting them more efficiently to π-stacking and/or other hydrophobic cluster within amyloid fibril. iAβ6 is a promising candidate for a lead compound.

A chimeric relaxin family peptide R3/I5, containing the B-chain of relaxin-3 and the A-chain of INSL5, was recombinantly prepared and site-specifically labeled at the A-chain N-terminus by a diethylenetriaminepentaacetic acid/europium moiety. The labeled peptide bound the relaxin family peptide receptors RXFP3 and RXFP4 with high binding affinities and low nonspecific binding, representing a valuable nonradioactive receptor-binding tracer. The present approach could also be adapted for preparing and labeling of other chimeric relaxin family peptides.

The interaction of bioactive endothelins (ETs) with oxidized low-density lipoprotein (ox-LDL) and its major lipid component lysophosphatidylcholine (LPC) was investigated by fluorescence spectroscopy and western blotting. These results indicate that ox-LDL may contain micelle-rich LPCs and that ETs may interact with the bioactive LPC micelles specifically. Further study of the interaction between ETs and LPC micelles contained in ox-LDL will provide important information on the development and progression of many inflammatory diseases, including atherosclerosis.

We demonstrate binding of the phage display-selected motif XHSXVH∅ to the catalytic domain of the peptidyl-prolyl-cis/trans-isomerase Par17 by NMR spectroscopy. Using chemical shift perturbation analysis, we propose that residues within the catalytic center of Par17 are involved in substrate recognition.

Replacement of Lys residue next to the scissile bond by azaglycine in the calpain substrate resulted in an inhibitory compound.

Peptides adsorption behavior depends on the type of the surface. Nisin adsorbs in higher amount on hydrophilic than hydrophobic surfaces and it adopts different interactions, distribution, conformation, and orientation on those type of surfaces. Such changes affect its antibacterial activity and determine thus the performance of antimicrobial surface.

In this paper, the effect of stirring on the fibrillization of three peptides was studied. When stirring is stopped, the fibrillization of amylin and insulin practically stopped, and the rate for Aβ₄₀ substantially decreased, whereas the fibrillization of Aβ₄₂ peptide continued to proceed with almost the same rate as in the agitated conditions. This ability of Aβ₄₂ fibrils to grow under quiescent conditions could be responsible for their high propensity to form pathological aggregates in vivo.