Hierarchical Self‐Assembly of Poly‐Pseudorotaxanes into Artificial Microtubules

Hierarchical self‐assembly of building blocks over multiple length scales is ubiquitous in living organisms. Microtubules are one of the principal cellular components formed by hierarchical self‐assembly of nanometer‐sized tubulin heterodimers into protofilaments, which then associate to form micron‐length‐scale, multi‐stranded tubes. This peculiar biological process is now mimicked with a fully synthetic molecule, which forms a 1:1 host‐guest complex with cucurbit[7]uril as a globular building block, and then polymerizes into linear poly‐pseudorotaxanes that associate laterally with each other in a self‐shape‐complementary manner to form a tubular structure with a length over tens of micrometers. Molecular dynamic simulations suggest that the tubular assembly consists of eight poly‐pseudorotaxanes that wind together to form a 4.5 nm wide multi‐stranded tubule.     

Polymerization of 2,4-hexadiyn-1,6-diol by chemical vapor deposition

2,4-Hexadiyn-1,6-diol (HDO) was polymerized on glass and silicon plates by chemical vapor deposition without transition metal catalysis to form homogeneous thin films. Structural properties of the films were investigated by FT-IR, UV-visible, Raman, x-ray diffraction, and XPS spectroscopic analyses. The structure of CVD-polymerized HDO (CVD-PHDO) films was different from that of metathesis polymerized HDO (metathesis-PHDO), showing a polyacene-based structure but no polyene structure with acetylenic side groups. © 1996 John Wiley & Sons, Inc.     

Electrochemical Detection of Lead Ion Based on a Peptide Modified Electrode

A novel biosensor harnessing a peptide layer which has specific affinity to lead ion proved to be highly effective for electrochemical analysis of lead ions. The peptide modified electrode was used for the electrochemical analysis of various trace metal ions by square wave voltammetry. Compared to the other ions investigated, the peptide modified electrode was found to be highly selective to Pb²⁺ in the range of 50–700 nM. Furthermore, the biosensor exhibited a high reusability and good spike recovery in the tap water containing various concentration of Pb²⁺.     

Apis mellifera syriaca Venom: Evaluation of Its Anticoagulant Effect,Proteolytic Activity,and Cytotoxicity along with Its Two Main Compounds—MEL and PLA2—On HeLa Cancer Cells

Bee venom (BV) is one of the most remarkable natural products that has been a subject of studies since ancient times. Recent studies have shown that Apis mellifera syriaca venom possesses antibacterial as well as cytotoxic effects on cancer cell lines. The venom contains a variety of bioactive molecules—mainly melittin (MEL) and phospholipase A2 (PLA2), as well as other compounds that are not well characterized. In this work, we continue the biological characterization of A. mellifera syriaca venom by testing its anticoagulant effect on human plasma using the prothrombin time (PT) test, as well as assessing its proteolytic activity. In addition, the cytotoxicity of the crude venom—and of its two main components, MEL and PLA2—was tested on HeLa cancer cell lines for the first time. The results obtained showed the capacity of A. mellifera syriaca venom to increase clotting time, thereby proving its anticoagulant effect. Moreover, the venom did not demonstrate a significant proteolytic activity unless administrated at concentrations ≥ 5 mg/mL. Finally, we showed that crude A. mellifera syriaca venom, along with MEL, exhibit a strong in vitro cytotoxic effect on HeLa cancer cell lines, even at low concentrations. In summary, our findings could serve as a basis for the development of new natural-based drug candidates in the therapeutic field.