NIST launch proteomics reference materials

By Dr Matt Wilkinson

- Last updated on GMT

Related tags Amino acid

The National Institute of Standards and Technology (NIST) has
issued its first ever reference material to improve the performance
and reliability of proteomics research.

The new reference material (RM), NIST RM 8327, was developed by the Association of Biomolecular Resource Facilities (ABRF) in collaboration with the NIST to act as a chemical ruler that peptide fragments can be measured against.

The ABRF is a non-profit international society created by representatives from industry, universities and government agencies to advance the output of biotechnology laboratories through research, communication and education and has recognised the need for such a material for some time.

Proteomics, the study of proteins, how they interact and their biological function, has become an important part of the drug discovery process and has been part of a radical change in both biological research and drug discovery.

It is estimated that there are between 10m and 20m proteins that interact in very complex networks to control cellular processes.

By gaining a better understanding of these processes researchers hope to be able to design new drugs that specifically target disease progression mechanisms.

The analysis of proteins is usually conducted by chopping them into small peptide fragments using protease enzymes before separating those using techniques such as high performance liquid chromatography (HPLC) or electrophoresis.

These peptides are then analysed by mass spectrometry (MS) to give the weight of the fragment.

There has been significant research into improving the amount of data collected during MS analysis, but one stumbling block has been the lack of a validated reference material.

The new reference material consists of three synthetic peptides that have lengths of 11, 14 and 26 amino acid residues and will cost $398 (€294) for the set.

The peptides were designed to be stable over a long length of time and therefore, do not contain methionine, cysteine or trypotphan that can compromise stability.

They contain a range of protease cleavage sites and contain tyrosine to enable accurate concentration analysis by UV spectroscopy - vital for validating the concentration of any standard solutions against which protein samples will be measured.

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