THE STUDY ON THE WATER SOLUBLE PEPTIDES IN PAPAVER SOMNIFERUM POLLEN EXTRACTION,PURIFICATION,SEQUENCE DETERMINATION AND SYNTHESIS

Four peptides PSPP1,PSPP2,PSPP3 and PSPP4 were purified from the water-extract of Papaver somniferum pollen.Their sequences,with 21,17,13 and 16 amino acid residues respectively,have been determined by Edman degradation-N-terminal dansylation.PSPP2, PSPP3 and PSPP4 were synthesized using solid phase method.The immunopromotive activities of PSPP1,PSPP2,PSPP3,PSPP4 and the initially separated sample PSPP have been also observed by the methods of counting erythrocyte rosette forming cells(ERFC) and T-lymphocyte transformation test in vitro.

Studies on Fragmentation of Peptide by Nano-electrospray Ionization Fourier Transform Ion Cyclotron Resonance Multi-stage Tandem Mass Spectrometry

The sequence analysis of peptides was performed by nano-electrospray ionization Fourier transform ion cyclotron resonance tandem mass spectrometry（Nano-ESI-FT-ICR-MSn） and several peptides were chosen as examples. With the aid of the collision induced dissociation（CID）, FT-ICR provides not only precise mass/charge ratio, but also structure information of the selected peptides. The fragment ions were identified according to the observed molecular weights and peptide sequence was determined successfully. So Nano-ESI-FT-ICR-MSn is a useful tool for identification of the amino acid sequence of peptides with high confidence. Besides, a pathway for the dehydration of y ions without amino acids containing carboxylic acid under sustained off-resonance irradiation collision-induced dissociation（SORI-CID） condition was proposed.

Synthesis and antiangiogenic activities of 5-amino-1,3-dihydro-1,3-dioxo-2H-isoindole-2-propanoic acid derivatives

Based on the structure-activity relationships and antiangiogenic mechanism of RGD-containing peptides, a series of 5-amino- 1,3-dihydro-1,3-dioxo-2H-isoindole derivatives were synthesized. The structures were characterized by ^1H NMR, MS and elementary analysis. There ability to inhibit angiogenesis were evaluated by chick embryo chorioallantoic membrane assay at 10^-5 mol/L. Compounds 7a and 7b displayed obvious antiangiogenic activity.

Amino acid identification and sequence analysis of peptides by reaction mass spectrometry

Fast atom bombardment mass spectrometry (FAB-MS) is applied to distinguish N- terminal series ions from C-terminal series ions of a peptide by on-probe acetylation, it provides valuable information about the sequence of an unknown peptide. The FAB mass spectra contain a number of characteristic ions at low-mass region in addition to the sequence ions at high-mass region. It was found that the ions below m/z 200 are characteristic of the amino acid composition of the peptide, from which the amino acid composition of the peptide could be estimated. Additionally, mixture analysis is also discussed.

Sequence modulation of tunneling barrier and charge transport across histidine doped oligo-alanine molecular junctions

Series tunneling across peptides composed of various amino acids is one of the main charge transport mechanisms for realizing the function of protein. Histidine, more frequently found in redox active proteins, has been proved to be efficient tunneling mediator. While how it exactly modulates charge transport in a long peptide sequence remains poorly explored. In this work, we studied charge transport of a model peptide junction, where oligo-alanine peptide was doped by histidine at different position,and the series of peptides were self-assembled into a monolayer on gold electrode with soft EGa In as top electrode to form molecular junction. It was found that histidine increased the overall conductance of the peptide, meanwhile, its position modulated the conductance as well. Quantitative analysis by transport model and ultraviolet photoelectron spectroscopy(UPS) indicated a sequence dependent energy landscape of the tunneling barrier of the junction. Density-functional theory(DFT) calculation on the electronic structure of histidine doped oligo-alanine peptides revealed localized highest occupied molecular orbital(HOMO) on imidazole group of the histidine, which decreased charge transport barrier.

Proteome-Based Clustering Approaches Reveal Phylogenetic Insights into Amphistegina

Foraminifera are highly diverse and have a long evolutionary history.As key bioindicators,their phylogenetic schemes are of great importance for paleogeographic applications,but may be hard to recognize correctly.The phylogenetic relationships within the prominent genus Amphistegina are still uncertain.Molecular studies on Amphistegina have so far only focused on genetic diversity within single species and suggested a cryptic diversity that demands for further investigations.Besides molecular sequencing-based approaches,different mass spectrometry-based proteomics approaches are increasingly used to give insights into the relationship between samples and organisms,especially as these do not require reference databases.To better understand the relationship of amphisteginids and test different proteomics-based approaches we applied de novo peptide sequencing and similarity clustering to several populations of Amphistegina lobifera,A.lessonii and A.gibbosa.We also analyzed the dominant photosymbiont community to study their influence on holobiont proteomes.Our analyses indicate that especially de novo peptide sequencing allows to reconstruct the relationship among foraminiferal holobionts,although the detected separation of A.gibbosa from A.lessonii and A.lobifera may be partly influenced by their different photosymbiont types.The resulting dendrograms reflect the separation in two lineages previously suggested and provide a basis for future studies.