New NIST reference material for peptide analysis

May 25, 2007

The National Institute of Standards and Technology (NIST) has issued its first-ever reference material designed to improve the performance and reliability of experiments to measure the masses and concentrations of peptides in biomolecular samples. The new reference material is expected to be an important tool in the analysis of proteins, both for disease diagnosis and drug discovery.

Proteomics—the study of proteins and the roles they play in biology—is one of the most fertile fields of modern medical research. Proteins typically are very large molecules, built of hundreds or thousands of amino acids, but they can be divided into smaller units, chains of about 50 or fewer amino acids. These are peptides. The usual way to analyze proteins is to chop them into their constituent peptides (generally with enzymes that cut through them at specific sites), sort the various peptides out using a chemical separation technique like high performance liquid chromatography (HPLC), and then determine the mass of each peptide using mass spectroscopy.

One big uncertainty in this process is that the peptide fragments differ in size, electrical charge and physical properties (such as the speed in which they separate under HPLC.) Chemists are accustomed to using well-known reference samples as chemical rulers to calibrate their analysis instrumentation, but until now there have been no such reference samples of peptides.

The need for this peptide reference material has been long recognized by the Association of Biomolecular Resource Facilities (ABRF), a non-profit standards organization created by representatives from industry firms, universities and government agencies. In collaboration with NIST, the ABRF created a Peptide Standards Project Committee to design and characterize three synthetic peptides to serve as the basis for a NIST peptide reference material. NIST RM 8327, "Peptide Reference Material for Molecular Mass and Purity Measurements," consists of three peptides from 11, 14 and 26 amino acid residues in length, with net charges of -3, -1 and +3. These three synthetic peptides were designed to provide long-term stability (do not contain methionine, cysteine and tryptophan), a range of purities, a range of molecular masses, protease cleavage sites, and contain tyrosine to enable concentration analysis by UV spectroscopy.

Source: National Institute of Standards and Technology (NIST)

Explore further: How can we avoid kelp beds turning into barren grounds?

add to favorites email to friend print save as pdf

Related Stories

Protein coding 'junk genes' may be linked to cancer

Nov 17, 2013

By using a new analysis method, researchers at Karolinska Institutet and Science for Life Laboratory (SciLifeLab) in Sweden have found close to one hundred novel human gene regions that code for proteins. A number of these ...

Recommended for you

Parasitic worm genomes: largest-ever dataset released

11 hours ago

The largest collection of helminth genomic data ever assembled has been published in the new, open-access WormBase-ParaSite. Developed jointly by EMBL-EBI and the Wellcome Trust Sanger Institute, this new ...

Male sex organ distinguishes 30 millipede species

11 hours ago

The unique shapes of male sex organs have helped describe thirty new millipede species from the Great Western Woodlands in the Goldfields, the largest area of relatively undisturbed Mediterranean climate ...

How can we avoid kelp beds turning into barren grounds?

15 hours ago

Urchins are marine invertebrates that mould the biological richness of marine grounds. However, an excessive proliferation of urchins may also have severe ecological consequences on marine grounds as they ...

User comments : 0

Please sign in to add a comment. Registration is free, and takes less than a minute. Read more

Click here to reset your password.
Sign in to get notified via email when new comments are made.