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N Winograd

Publications and source records attributed to N Winograd.

36 records · Page 2Linked to original sources

Imaging with ion beams and laser postionization.

We investigate the use of a liquid metal ion gun (LMIG) combined with multiphoton resonance ionization of sputtered atoms and/or molecules to acquire mass-selected images with submicrometer spatial resolution. Images from several model systems are presented including those of an In grid, and of patterned surfaces of benzo[a]pyrene and tryptophan thin films. Since postionization for these systems yields ionization efficiencies that are considerably higher than those achieved with secondary ion mass spectrometry (SIMS), spatial resolution of 2600 A for molecular species could be achieved while static conditions were maintained. Cooling of the sample to < 210 K was shown to be essential for molecular systems since the number of thermally evaporating molecules overwhelms the number of sputtered molecules at room temperature. Other details necessary to incorporate laser postionization into a time-of-flight SIMS instrument using a pulsed LMIG source are also discussed.

Benzo(a)pyrene↗

A mass spectrometric solution to the address problem of combinatorial libraries.

The molecular weights of femtomole quantities of small peptides attached to polystyrene beads have been determined with imaging time-of-flight secondary ion mass spectrometry. The analysis is made possible by the selective clipping of the bond linking the peptide to a bead with trifluoroacetic acid vapor before the secondary ion mass spectrometry assay. The approach can be applied to large numbers of 30- to 60-micrometer polystyrene beads for the direct characterization of massive combinatorial libraries.

Amino Acid Sequence↗

Analyses of cryogenic samples using ion-induced desorption and multiphoton resonance ionization.

In this study, ion-beam-induced desorption with multiphoton resonance ionization detection of desorbed neutral molecules is used to characterize frozen aqueous solutions. This type of matrix is of particular importance since it serves as a model for biological matrices. The time-of-flight mass spectrum, obtained in this way for a millimolar tryptophan/H2O solution, is virtually identical to that for a submonolayer of tryptophan on a silicon wafer. The tryptophan signal from a frozen solution is demonstrated to have a linear dependence on concentration by using 4,4'-biphenyldiol as an internal standard. A detection limit of 2 x 10(-6) M is also demonstrated. Since our ion beam samples one layer of 0.1 cm2 and we assume 10(15) molecules/cm2 of ice, this concentration corresponds to approximately 4 x 10(6) molecules/layer. It is also shown that the signal exhibits an exponential decay with primary ion dose due to the accumulation of primary ion damage in the near-surface molecules.

Freezing↗

Detection of biomolecules on surfaces using ion-beam-induced desorption and multiphoton resonance ionization.

Multiphoton resonance ionization (MPRI) has been combined with ion-beam-induced desorption to examine a set of thermally labile biological molecules present on surfaces. Specifically, we have examined films of adenine and beta-estradiol, molecules with a rigid skeletal backbone. In both of these cases, molecular ions could be produced efficiently without cooling the neutral molecules into their ground vibrational state. We have also studied other more fragile molecules such as tryptamine, tryptophan, phenylalanine, and serotonin. The base peak in the mass spectra of these molecules is fragment ions formed by losses of the amine side chains. Even with this fragmentation, however, it is possible to achieve sensitivity limits that are many orders of magnitude greater than for secondary ion mass spectrometry, without preparing the samples in special matrices. For serotonin, detection limits of 40 fmol on the surface of a silicon target are achievable. The results also yield a linear relation between the serotonin base fragment ion intensity and the known surface concentration.

Adenine↗