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: Zimbabwe to export elephants in population curb

add to favorites email to friend print save as pdf

Related Stories

Nanodot team aims to charge phones in less than a minute

Nov 25, 2014

The world of smartphone users, which is a very large base indeed, is ripe for better battery solutions and an Israel-based company has an attractive solution in store, in the form of nanodot batteries that ...

Recommended for you

Research sheds light on what causes cells to divide

22 hours ago

When a rapidly-growing cell divides into two smaller cells, what triggers the split? Is it the size the growing cell eventually reaches? Or is the real trigger the time period over which the cell keeps growing ...

Locking mechanism found for 'scissors' that cut DNA

22 hours ago

Researchers at Johns Hopkins have discovered what keeps an enzyme from becoming overzealous in its clipping of DNA. Since controlled clipping is required for the production of specialized immune system proteins, ...

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.