History and Introduction of Mass Spectrometry (MS)
History and Introduction of Mass Spectrometry (MS) |
Table of Contents
- History
- Introduction
- Principle
- Instrumentation
- Mass spectrum
- Applications
History
The earliest gas discharge experiments served as the
foundation for mass spectrometry. This were carried out in a glass tube that
had been partially emptied and into which electrodes had been placed. A number
of glowing light phenomena were seen when the gas pressure and voltage across
the electrodes were appropriate.
Wilhelm Wien, a German scientist, discovered in 1898
that charged particle beams could be deflected by a magnetic field, which
established the groundwork for mass spectroscopy. British physicist J.J.
Thomson, who had previously discovered the electron and seen its deflection
through an electric field, conducted more complex experiments between 1907 and
1913 in which he passed a beam of positively charged ions throughout a combined
magnetic and electrostatic field.
The two fields in Thomson's tube were positioned so
that the ions were diverted in two perpendicular directions through tiny
angles. In the end, the ions caused a series of parabolic curves to appear on a
photographic plate that was in their path. Each parabola represented ions with
a given mass-to-charge ratio, with the position of each ion depending upon the
velocity. The lengths of the parabolic curves served as a measurement for the
range of ion energies present in the beam. And afterwards, Thomson swapped out
the photographic plate for a metal sheet that had a parabolic slit cut into it
in an effort to assess the relative abundances of the various ion species
present.
He was able to measure a current related to each
distinct ion species by changing the magnetic field while going through a mass
spectrum. As a result, he can be given credit for creating the first mass
spectrograph and mass spectrometer.
Introduction
Mass spectrometry is a potent analytical technique
that may be used to analyze known materials, detect unknown elements in a
sample, and provides insight on the structure and chemical characteristics of
various molecules. The entire procedure entails converting the sample into
gaseous ions, with or without fragmentation, and characterizing those ions
according to their relative abundances and mass to charge ratios (m/z).
This method essentially investigates how molecules are
affected by ionizing energy. The consumption of sample molecules during the
creation of ionic and neutral species depends on chemical events occurring in
the gas phase.
Principle
A sample, which could be solid, liquid, or gas, is
ionized during a conventional Mass Spectrometry operation, for example by being
bombarded with an electron beam. This could result in some of the molecules in
the sample fragmenting into positively charged parts or just becoming
positively charged as a whole. Afterwards, these
ions (fragments) are separated based on their mass-to-charge ratio, by
accelerating them and exposing them to an electric or magnetic field; ions with
the same mass-to-charge ratio will deflect equally. A system that can detect
charged particles, such as an electron multiplier, is used to find the ions.
Findings are shown as spectra of the detected ion signal strength as a function
of mass-to-charge ratio. By comparing known masses (such as the mass of a
complete molecule) to the identified masses or using a distinctive
fragmentation pattern, it is possible to identify the atoms or molecules in the
sample. A mass spectrometer exploits this characteristic of matter to map ions
of different masses on a mass spectrum, which is based on Newton's second law
of motion and momentum.
Instrumentation of Mass Spectrometry
It consists of four basic parts that are as follows,
1. Ionization Chamber
Ionizer - The electrons use bombardment to ionize the
sample. Between the cathode and the anode, these electrons move. High-energy
electrons knock electrons out of the sample as it passes through the electron
stream between the cathode and anode, forming ions.
2. Accelerating Plates
Ions put between a pair of charged parallel plates in
an accelerator are drawn to one plate and repelled by the other plate. By
altering the charge on the plates, the acceleration speed may be managed.
3. Deflector
Ions are deflected by a magnetic field depending on
their mass and charge. The least deflected ions are those that are big or have
two or more positive charges. The most ion deflection occurs when an ion is
light or has a single positive charge.
4. Detector
The right-charged and right-mass ions travel to the
detector. The ion that strikes the detector is used to examine the mass to
charge ratio.
Instrumentation |
Mass Spectrum
A graph of the ion signal as a function of the
mass-to-charge ratio is known as a mass spectrum. The masses of particles and
molecules in a sample, as well as the chemical identity or structure of
molecules and other chemical compounds, are all determined using these spectra.
Molecular Ion Peak
The peak that formed due to the removal of electrons
from actual molecule during the process ionization, its m/z value is same as
the mass of actual molecule. It is represented as M+ Peak. The peak that corresponds to the heaviest ion is
called the molecular ion peak.
A molecular ion
is created when an electrically neutral molecule releases one of its electrons.
A group of two or more atoms that are covalently linked together or a metal
complex that functions as a single entity and has a net charge that is greater
than zero are referred to as molecular ions. The mass of a molecular ion is
regarded as being equal to the mass of the molecule because the electron mass
is so little in comparison to that of a molecule.
Base Peak
The tallest
peak in the spectrum that shows 100% abundance is known as base peak. The ion that is most prevalent and plentiful is
represented by the base peak.
Example
The molecular mass of pentane is 72, so the peak at 72
is the molecular ion peak and tall peak that have 100 % abundance on y-axis is
known as base peak as shown in figure.
Mass Spectrum of Pentane |
Applications of Mass Spectrometry
- The pharmaceutical sector values the use of mass spectrometry (MS) for biochemical applications. These consist of techniques for measuring molecular functions such ligand binding as well as compositional assessments of biomolecules, particularly proteins.
- Cataloging protein expression, describing protein interactions, and locating protein modification sites are the three main uses of MS in proteomics.
- Uses of mass spectrometry in pharmaceutical analysis include metabolite screening, preclinical development, pharmacokinetic and pharmacodynamics assessments, drug discovery, and absorption, distribution, metabolism, and elimination (ADME) research.
No comments:
Post a Comment