Aminoalkyl derivatives of 2,4′-bithiazole-4-carboxylic acid,the intercalating part of bleomycin

The synthesis of three 2,4′-bithiazole derivatives related to the antibiotic antitumor bleomycin is reported. These compounds substituted by aminoalkyl chains on 2′ and/or 4-positions were prepared by the Hantzs synthesis between new thioamides and methyl 2-(2-bromoacetyl)thiazole-4-carboxylate and will be useful for the study of the intercalative moiety of bleomycin.     

Volatile compounds from the integument of White Leghorn Chickens (Gallus gallus domesticus L.): candidate attractants of ornithophilic mosquito species

Candidate kairomones of ornithophilic mosquito species are reported from GC/MS analysis of compounds from the skin on the back, the feet, and feathers from the back of White Leghorn chickens (Gallus gallus domesticus). Hexane and ether extracts of chicken feathers differ significantly in attractiveness of Culex spp. mosquitoes. The active (hexane) extracts contained an abundance of alcohols, ketones, and diones. The inactive (ether) extracts contained aldehydes, which also were in the hexane extracts. Analysis of hexane extracts from chicken feet, skin, and feathers demonstrated the qualitative similarity in the compounds collected with subtle differences observed in the quantitative amounts of these compounds. Aldehydes and carboxylic acids were detected in a concentrated ether extract of feathers in quantitatively similar ratios within each compound class for the corresponding series of C(6)-C(9 )aldehydes and acids.     

Gas chromatography/mass spectrometry analysis of the cuticular hydrocarbons from parasitic wasps of the genus Muscidifurax

Parasitic Hymenoptera can be difficult to identify by conventional taxonomic techniques. Examination of the cuticular hydrocarbons (CHCs) provides a basis for chemotaxonomic differentiation, which may lead to the discovery of pheromones, and can be a means of examining colonies for species cross-contamination. The parasitic wasps examined were Muscidifurax raptor, M. zaraptor, M. uniraptor, and the gregarious form of M. raptorellus. Species within the genus Muscidifurax, as well as the sex, can clearly be differentiated by examining the gas chromatograms of the CHCs. Identification of the alkanes by mass spectrometry shows uncommon dimethylalkanes and trimethylalkanes for members of the genus. The methyl branched cuticular hydrocarbons of these insects are rare compared to those found on insects reported in the literature, but are present in significant amounts on these insects. Additionally, sexual dimorphism is observed in long chain alkanes (C₂₁–C₃₉) present on male and female cuticular surfaces for these species. Females tend to have cuticular hydrocarbons with methyl branches located externally on the carbon backbone chain for dimethyl-, trimethyl-, and tetramethylalkanes, whereas males tend to have dimethyl- and trimethylalkanes located internally on the hydrocarbon backbone chains. Mass spectra of novel and rare methyl branched compounds identified on these parasitoids are presented.     

GC-MS analysis of cuticular lipids in recent and older scavenger insect puparia. An approach to estimate the postmortem interval (PMI)

An analytical method was developed to characterize puparia cuticular lipids (hydrocarbons, waxes) and to compare the molecular distribution patterns in the extracts from either recent or older puparia. Acid-catalyzed transesterification and solvent extraction and purification, followed by combined gas chromatography coupled to mass spectrometry, were optimized for the determination of hydrocarbons and fatty acid ethyl esters from transesterified waxes, extracted from a single species of a fly scavenger (Hydrotaea aenescens Wiedemann, 1830). Comparison between recent (2012) or older (1997) puparia contents has highlighted significant composition differences, in particular, a general decrease of the chain length in the n-alkane distribution pattern and, on the contrary, an increase of the ester chain length. Both extracts contain traces of three hopane hydrocarbon congeners. Preliminary results evidence the change in puparia lipid composition over time, thus potentially providing new indices for estimating postmortem interval.     

Investigations of the Mechanism of the “Proline Effect” in Tandem Mass Spectrometry Experiments: The “Pipecolic Acid Effect”

The fragmentation behavior of a set of model peptides containing proline, its four-membered ring analog azetidine-2-carboxylic acid (Aze), its six-membered ring analog pipecolic acid (Pip), an acyclic secondary amine residue N-methyl-alanine (NMeA), and the D stereoisomers of Pro and Pip has been determined using collision-induced dissociation in ESI-tandem mass spectrometers. Experimental results for AAXAA, AVXLG, AAAXA, AGXGA, and AXPAA peptides are presented, where X represents Pro, Aze, Pip, or NMeA. Aze- and Pro-containing peptides fragment according to the well-established “proline effect” through selective cleavage of the amide bond N-terminal to the Aze/Pro residue to give y_n ⁺ ions. In contrast, Pip- and NMA-fragment through a different mechanism, the “pipecolic acid effect,” selectively at the amide bond C-terminal to the Pip/NMA residue to give b_n ⁺ ions. Calculations of the relative basicities of various sites in model peptide molecules containing Aze, Pro, Pip, or NMeA indicate that whereas the “proline effect’ can in part be rationalized by the increased basicity of the prolyl-amide site, the “pipecolic acid effect” cannot be justified through the basicity of the residue. Rather, the increased flexibility of the Pip and NMeA residues allow for conformations of the peptide for which transfer of the mobile proton to the amide site C-terminal to the Pip/NMeA becomes energetically favorable. This argument is supported by the differing results obtained for AAPAA versus AA(D-Pro)AA, a result that can best be explained by steric effects. Fragmentation of pentapeptides containing both Pro and Pip indicate that the “pipecolic acid effect” is stronger than the “proline effect.” Figure

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Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins

Membrane binding of proteins such as short chain dehydrogenase reductases or tail-anchored proteins relies on their N- and/or C-terminal hydrophobic transmembrane segment. In this review, we propose guidelines to characterize such hydrophobic peptide segments using spectroscopic and biophysical measurements. The secondary structure content of the C-terminal peptides of retinol dehydrogenase 8, RGS9-1 anchor protein, lecithin retinol acyl transferase, and of the N-terminal peptide of retinol dehydrogenase 11 has been deduced by prediction tools from their primary sequence as well as by using infrared or circular dichroism analyses. Depending on the solvent and the solubilization method, significant structural differences were observed, often involving α-helices. The helical structure of these peptides was found to be consistent with their presumed membrane binding. Langmuir monolayers have been used as membrane models to study lipid–peptide interactions. The values of maximum insertion pressure obtained for all peptides using a monolayer of 1,2-dioleoyl-sn-glycero-3-phospho-ethanolamine (DOPE) are larger than the estimated lateral pressure of membranes, thus suggesting that they bind membranes. Polarization modulation infrared reflection absorption spectroscopy has been used to determine the structure and orientation of these peptides in the absence and in the presence of a DOPE monolayer. This lipid induced an increase or a decrease in the organization of the peptide secondary structure. Further measurements are necessary using other lipids to better understand the membrane interactions of these peptides.