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MALDI Analysis (maldi + analysis)

Distribution by Scientific Domains

Chemistry	50%

Selected Abstracts

MALDI analysis of presolar nanodiamonds: Mass spectrometric determination of the mass distribution of nanodiamonds from meteorites and a technique to manipulate individual nanodiamonds

METEORITICS & PLANETARY SCIENCE, Issue 7 2005
Ian C. LYON
The techniques used to prepare and mass analyze nanodiamond samples from the Murchison (CM2) and Allende (CV3) meteorites are described. The mass spectra of nanodiamonds (peaking at between 1 times 104 -1.5 times 104 Daltons) are compared with size distributions obtained by point-counting transmission electron microscopy (TEM) images obtained elsewhere and reasonable agreement is found. The implications of the ability to produce and mass analyze a beam of nanodiamonds are explored. [source]

Off-line liquid chromatography-MALDI by with various matrices and tandem mass spectrometry for analysis of glycated human serum albumin tryptic peptides

MOLECULAR NUTRITION & FOOD RESEARCH (FORMERLY NAHRUNG/FOOD), Issue 4 2007
Annunziata Lapolla
Abstract Advanced glycation end-product (AGE)/peptides, arising from in vivo digestion of glycated proteins, are biologically important compounds, due to their reactivity against circulating and tissue proteins. For information on their possible structure, in vitro glycation of HSA and its further enzymatic digestion were performed. The resulting digestion product mixture was analysed directly by MALDI MS with various matrices [2,5-dihydroxy benzoic acid (DHB) and ,-cyano-4-hydroxy cinnamic acid (CHCA)]. Alternatively, offline microbore LC prior to MALDI analysis was used, and showed that 63% of the free amino groups prone to glycation are modified, indicating the contemporary presence of unglycated peptides. This result proves that, regardless of the high glucose concentration employed for HSA incubation, glycation does not go to completion. Further studies showed that the collisionally activated decomposition of singly charged glycated peptides leads to specific fragmentation pathways, all related to the condensed glucose molecule. These unique product ions can be used as effective markers to establish the presence of a glucose molecule within a peptide ion. [source]

Detergent addition to tryptic digests and ion mobility separation prior to MS/MS improves peptide yield and protein identification for in situ proteomic investigation of frozen and formalin-fixed paraffin-embedded adenocarcinoma tissue sections

PROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 10 2009
Marie-Claude Djidja
Abstract The identification of proteins involved in tumour progression or which permit enhanced or novel therapeutic targeting is essential for cancer research. Direct MALDI analysis of tissue sections is rapidly demonstrating its potential for protein imaging and profiling in the investigation of a range of disease states including cancer. MALDI-mass spectrometry imaging (MALDI-MSI) has been used here for direct visualisation and in situ characterisation of proteins in breast tumour tissue section samples. Frozen MCF7 breast tumour xenograft and human formalin-fixed paraffin-embedded breast cancer tissue sections were used. An improved protocol for on-tissue trypsin digestion is described incorporating the use of a detergent, which increases the yield of tryptic peptides for both fresh frozen and formalin-fixed paraffin-embedded tumour tissue sections. A novel approach combining MALDI-MSI and ion mobility separation MALDI-tandem mass spectrometry imaging for improving the detection of low-abundance proteins that are difficult to detect by direct MALDI-MSI analysis is described. In situ protein identification was carried out directly from the tissue section by MALDI-MSI. Numerous protein signals were detected and some proteins including histone H3, H4 and Grp75 that were abundant in the tumour region were identified. [source]

Using sol,gel/crown ether hybrid materials as desalting substrates for matrix-assisted laser desorption/ionization analysis of oligonucleotides

RAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 13 2004
Mao-Feng Weng
This study demonstrates the feasibility of using sol,gel/crown ether hybrid materials as sample substrates that reduce the intensity of the signals of sodium ion adducts of oligonucleotides during matrix-assisted laser desorption/ionization (MALDI) analysis. 2-Hydroxymethyl[15]crown-5 and 2-hydroxymethyl[18]crown-6 were added as dopants during the sol,gel process to generate desalting substrates for MALDI sample deposition. The results demonstrate that the sol,gel/crown ether hybrid materials effectively suppress the formation of sodiated oligonucleotides during MALDI analysis. The largest detectable molecular size for an oligonucleotide was a 100-mer, and the detection limit for an oligonucleotide 36-mer was ca. 20,fmol. Copyright © 2004 John Wiley & Sons, Ltd. [source]

Analysis of a bioactive , -(1,,,3) polysaccharide (Curdlan) using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

RAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 9 2003
T.-W. D. Chan
This paper focuses on the development of MALDI sample preparation protocols for the analysis of a bioactive , -(1,,,3) polysaccharide, i.e. Curdlan. The crude Curdlan sample was first separated into a low molecular weight water-soluble portion and a high molecular weight water-insoluble portion. The water-soluble portion was analyzed using a standard MALDI sample preparation method developed for dextran analysis. Two low-mass (<4000,Da) polysaccharide distributions differing by 16,Da were observed. For the analysis of the water-insoluble portion, several sample preparation protocols were evaluated using GPC-fractionated samples. A sample preparation method based on the deposition of the analyte solution with a mixture of 2,5-dihydroxybenzoic acid (DHB) and 3-aminoquinoline (3AQ) matrices in dimethyl sulfoxide (DMSO) at elevated temperature of 70°C was found to reliably produce good MALDI spectra. MALDI analysis of the water-insoluble Curdlan portion gave number-average (Mn) and weight-average (Mw) molecular weights and polydispersity of 8000,Da, 8700,Da, and 1.10, respectively. Copyright © 2003 John Wiley & Sons, Ltd. [source]

Lipid-transfer proteins as potential plant panallergens: cross-reactivity among proteins of Artemisia pollen, Castanea nut and Rosaceae fruits, with different IgE-binding capacities

CLINICAL & EXPERIMENTAL ALLERGY, Issue 10 2000
A. DÍaz-Perales
Background Lipid-transfer proteins (LTPs), but not Bet v 1 homologues, have been identified as major allergens of apple and peach in the Rosaceae fruit-allergic population in the Mediterranean area. Many of these patients show cosensitization to mugwort pollen. LTPs have an ubiquitous distribution in tissues of many plant species, and have been proposed as a novel type of plant panallergens. Objective We sought to isolate LTPs from Artemisia pollen and from a plant food not belonging to the Rosaceae family, such as chestnut nut, and to compare their amino acid sequences and IgE-binding capacities with those of apple and peach LTPs. Methods Allergens (LTPs) were isolated by different chromatographic methods (gel-filtration, ion exchange and/or reverse-phase HPLC), and characterized by N-terminal amino acid sequencing and MALDI analysis. Specific IgE-quantification and immunodetection, as well as immunoblot and ELISA inhibition assays, were carried out using sera from patients allergic to both apple and peach. Results Purified LTPs from Artemisia pollen and from chestnut seed showed molecular masses about 9 700d, and 43,50% sequence identity with the equivalent allergens of apple and peach in the first 30 N-terminal residues, which comprise about one third of the total amino acid sequence. A similar degree of sequence identity (50%) was found between the Artemisia and chestnut proteins. Both isolated LTPs bound specific IgE of sera from Rosaceae fruits allergic patients. However, substantially lower values of specific IgE-binding and maximum ELISA inhibition percentages were obtained for Artemisia and chestnut LTPs when compared to those from apple and peach. Conclusion LTPs from Artemisia pollen and chestnut crossreact with allergens (LTPs) of Rosaceae fruits, but significant differences in specific IgE-binding capacities were observed among members of the plant LTP family. Thus, further studies are needed to evaluate the clinical significance of the observed cross-reactivities of plant LTPs. [source]