Bis-coupling of peptide to α-cyclodextrin by the Huisgen reaction was reported provided long enough linker was used. The resulting conjugates display a propensity to form α-helix in water.

The novel stilboflavin C peptides, namely ten 16-residue and five 19-residue sequences, were isolated from submerged cultures of the fungus Stilbella flavipes CBS 146.81 (Image: the species growing on a fallen tree, white scale bar: 1 mm). These peptides contain Ser-Alaol or Ser-Leuol, which are rarely found as C-termini, as well as repetitive motifs (Leu-Aib-Gly)2,3 which have not been detected in peptaibols before.

Solid phase cyclodimerization of VPRSGEVYT sequence using polyethylene glycol for head-to-head and (Gly₅)₂-Lys spacer for tail-to-tail cyclization resulted in a 132 atom macrocycle with enhanced immunosuppressive activity. The structure of cyclodimer was unambiguously confirmed by detailed ESI-MS/MS analysis.

Human osteoclast-stimulating factor (hOSF) is an intracellular protein produced by osteoclasts that induces osteoclast formation and bone resorption. Here, we report rational design of the peptoid ligands of hOSF SH3 domain by integrating computational biology analysis and fluorescence binding assay. Consequently, two designed peptoid molecules with proline residue replaced separately by N-substituted amino acids N-Clp and N-Ffa are identified to have a satisfactory affinity profile towards hOSF SH3 domain.

Herein, we report a facile method to construct thioether-tethered cyclic peptides via intra-molecular thiol–ene reaction. This reaction is highly efficient and selective with satisfying residue compatibility.

The synthesis and the potency and selectivity of new dermorphin analogues is described. The most active analogue in this series, Tyr-(R)-Ala-(R)-α-benzyl-β-azidoAla-Gly-Tyr-Pro-Ser-NH₂ and its epimer were analyzed by ¹H and ¹³C NMR spectroscopy and restrained MD simulations.

Confocal laser scanning microscopy image of Detroit-562 human pharynx tumour cells (blue) after 5 h of incubation with 10 μM Lys⁸(FITC)]-GnRH-III (green).

Selectively labelled fluorescent GnRH-I, -II and -III derivatives are reliable tools for tracking and quantifying their receptor-mediated cellular uptake in vitro and able to predict the corresponding GnRH-drug conjugate tumour targeting efficiency in vivo.

We demonstrate for the first time that human pharynx tumour (Detroit-562) cells highly express GnRH-I receptors on their surface. Cellular uptake experiments with these labelled GnRH conjugates proved that the transport for each of the three GnRH analogues into Detroit-562 cells is efficiently mediated by the GnRH-I receptor.