Conformational investigations on glycosylated asparagine-oligopeptides of increasing chain length.

Stepwise solution syntheses of the homo-oligomers Boc-(Asn)n-NHCH3 (n = 1-5; I1-5), Boc-[[GlcNAc(Ac)3beta]Asn]n-NHCH3 (n = 1-8; II1-8), and Boc-[(GlcNAcbeta)Asn]n-NHCH3 (n = 1-8; III1-8) are described. Members of the series III were obtained by deacetylation of the corresponding members of the series II. The conformational preferences of the N-protected homo-peptides of the three series were investigated by spectroscopic techniques. 1H-NMR measurements were carried out in various solvents; the CD spectra were recorded in water, aqueous SDS and TFE. The poor solubility of the oligomers of the three series prevented FT-IR measurements in solution. NMR and IR measurements indicate the existence of unordered structures containing some gamma-turns in the carbohydrate-free oligomers and the presence of beta-turns in the glycosylated oligopeptides, whether acetylated or not. The CD spectra do not indicate the presence of organized structures. The sugar moieties apparently do not have a structure-inducing effect on the asparagine homo-oligomer main chain.     

Spindle activity during sleep in subjects with a deficit in pallesthetic sensibility

Sleep spindle activity was studied on four subjects affected by pallesthesic deficit due to injury the posterior funiculi of the cord. The spindle activity was studied as density (number of spindles min.), duration and percent of sleep time utilized in spindle activity. The polygraph sleep records included EOG, EMG and 6 monopolar EEG recordings, 3 for each side, on the frontal, parietal and occipital regions. The records showed a spindle activity which was similar in different subjects and that was significantly higher than the physiological values. In fact, the spindle density was about 250%, the duration was about 130% and the spindle percent was about 280%, with respect to the physiological values assumed to be 100%.     

Synthesis of novel nitric oxide (NO)-releasing esters of timolol

A novel class of timolol derivatives with nitric oxide (NO)-donating moieties achieved chemical stability yet under physiologically relevant conditions released timolol and NO. Hindered esters A were designed and synthesized, whose ‘triggered’ release relied on enzymatic hydrolysis of the nitrate ester in A to B, that in turn cyclized to liberate timolol.     

New syntaxa for the prodrome of Italian vegetation

The aim of this study is to provide new syntaxa for the Italian vegetation checklist. For the class Rhamno–Prunetea which includes the class Paliuretea the new alliance Rhamno saxatilis–Paliurion spinae-christi is described, that is included in the order Paliuretalia spinae-christi with a central-western Mediterranean and sub-Mediterranean distribution. Otherwise, the more thermophilous Paliurus spina-christi vegetation is included in the new suballiance named as Oleo sylvestris–Paliurenion spinae-christi within the alliance Oleo–Ceratonion of the class Quercetea ilicis. For the class Trifolio–Geranietea medii, a new alliance named Hyperico calabricae–Asphodelion macrocarpi is proposed here.     

Fluorescent, internally quenched, peptides for exploring the pH-dependent substrate specificity of cathepsin B.

Cathepsin B is a cysteine protease that in tumor tissues is localized in both acidic lysosomes and extracellular spaces. It can catalyze the cleavage of peptide bonds by two mechanisms: endoproteolytic attack with a pH optimum around 7.4, and attack from the C-terminus with a pH optimum at 4.5-5.5. In this work, seven fluorescent, internally quenched, decapeptides have been synthesized using the prototypical cathepsin B selective substrate Z-Phe-Arg-AMC as a lead, and used to identify the structural factors determining the susceptibility of peptides to hydrolysis at acidic and neutral pH values. Each peptide differs from the others in one amino acid (residue 6) and contains a highly fluorescent Nma group linked to the alpha-amino function of the N-terminal Orn residue and a Dnp group linked to the side chain of the Lys(8) residue acting as a quencher. Proteolytic cleavage was monitored by measuring the increase of fluorescence at 440 nm upon excitation at 340 nm, and the cleavage sites were determined by HPLC followed by ESI-MS analysis. Peptides containing Ala or Phe at position 6 are good substrates for the enzyme at both pH 5.0 and 7.4. By contrast, those containing Glu, Asp, Lys or Val are not cleaved at all by cathepsin B at pH 7.4, and are poorly hydrolyzed at pH 5.0. These findings provide new information for the rational design of cathepsin B-activated peptide-containing anticancer drugs.