If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)

ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.


Analytical Chemistry

2-D NMR Assesses Biosimilar Structure

Drug Development: Interlaboratory study uses NMR to compare structures of filgrastim and three biosimilar versions

by Celia Henry Arnaud
February 15, 2016 | A version of this story appeared in Volume 94, Issue 7

Before a biosimilar version of a protein therapeutic drug can be approved, the manufacturer of the new product must demonstrate that its properties and activity are comparable to the original drug. Determining higher order protein structure is an important part of establishing biosimilarity. In an interlaboratory study, researchers at the U.S. Food & Drug Administration, Health Canada, the National Institute of Standards & Technology, and the Medical Products Agency of Sweden show that two-dimensional NMR is reliably precise enough for the job (Nat. Biotechnol. 2016, DOI: 10.1038/nbt.3474). The researchers visually compared the similarity of spectral patterns and also used statistical methods to compare the chemical shifts of each signal from 2-D NMR experiments run on different instruments for the brand-name drug Neupogen, generically known as filgrastim, and three biosimilar versions. The precision across six spectrometers in four labs was found to be better than 10 ppb and almost as good as the digital resolution of the measurement. The use of 2-D NMR to analyze original protein drugs and subsequent biosimilars will give regulatory authorities greater assurance of drug quality, the study’s authors note.


This article has been sent to the following recipient:

Chemistry matters. Join us to get the news you need.