RESUMO
Lignin is the natural binder in wood and lignocellulosic plants and is regarded as the main natural and renewable source of phenolic compounds. Its incorporation in the composition of fiberboards will enhance both the environmental performance of the panels and the complex use of natural resources. In recent years, the increased valorization of hydrolysis lignin in value-added applications, including adhesives for bonding fiberboard panels, has gained significant research interest. Markedly, a major drawback is the retention of lignin in the pulp until the hot-pressing process. This problem could be overcome by using a small content of phenol-formaldehyde (PF) resin in the adhesive mixture as an auxiliary binder. The aim of this research work was to investigate and evaluate the effect of the hot-pressing temperature, varied from 150 °C to 200 °C, in a modified hot-press cycle on the main physical and mechanical properties of fiberboard panels bonded with unmodified technical hydrolysis lignin (THL) as the main binder and PF resin as an auxiliary one. It was found that panels with very good mechanical properties can be fabricated even at a hot-pressing temperature of 160 °C, while to provide the panels with satisfactory waterproof properties, it is necessary to have a hot-pressing temperature of at least 190 °C.
RESUMO
BACKGROUND: Bioconjugates are promising alternatives for the multiple targeting of any disease. Pyrrole heterocycle is well known with many activities and is a building block of a lot of medical drugs. On the other hand, peptides are short molecules with many advantages such as small size, ability to penetrate the cell membrane and bond-specific receptors, vectorizing potential, etc. Thus, hybrid molecules between peptide and pyrrole moiety could be a promising alternative as an anti-pain tool. METHODS: New bioconjugates with a general formula Pyrrole (α-/ß-acid)-FELL-OH (NH2) were synthesized using Fmoc/OtBu peptide synthesis on solid support. HPLC was used to monitor the purity of newly synthesized bioconjugates. Their structures were proven by electrospray ionization mass spectrometry. The Paw Pressure test (Randall-Selitto test) was used to examinate the analgesic activity. Hydrolytic stability of targeted structures was monitored in three model systems with pH 2.0, 7.4 and 9.0, including specific enzymes by means of the HPLC-UV method. RESULTS: The obtained results reveal that all newly synthesized bioconjugates have analgesic activity according to the used test but free pyrrole acids have the best analgesic activity. CONCLUSIONS: Although free pyrrole acids showed the best analgesic activity, they are the most unstable for hydrolysis. Combination with peptide structure leads to the hydrolytic stabilization of the bioconjugates, albeit with slightly reduced activity.
RESUMO
BACKGROUND: The inflammatory process represents a specific response of the organism's immune system. More often, it is related to the rising pain in the affected area. Independently of its origin, pain represents a complex and multidimensional acute or chronic subjective unpleasant perception. Currently, medical doctors prescribe various analgesics for pain treatment, but unfortunately, many of them have adverse effects or are not strong enough to suppress the pain. Thus, the search for new pain-relieving medical drugs continues. METHODS: New tetrapeptide analogs of FELL with a generaanalgesic-Glu-X3-X4-Z, where X = Nle, Ile, or Val and Z = NH2 or COOH, containing different hydrophobic amino acids at positions 3 and 4, were synthesized by means of standard solid-phase peptide synthesis using the Fmoc/OtBu strategy in order to study the influence of structure and hydrophobicity on the analgesic activity. The purity of all compounds was monitored by HPLC, and their structures were proven by ESI-MS. Logp values (partition coefficient in octanol/water) for FELL analogs were calculated. Analgesic activity was examined by the Paw-pressure test (Randall-Selitto test). RESULTS: The obtained results reveal that Leu is the best choice as a hydrophobic amino acid in the FELL structure. CONCLUSIONS: The best analgesic activity is found in the parent compound FELL and its C-terminal amide analog.
