Characterizing Collagen at the Double

Conceived in the late 1980s, two-dimensional Fourier transform ion cyclotron resonance mass spectrometry (2D FT-ICR MS) correlates the mass-to-charge (m/z) ratio of fragment and precursor ions in a single spectrum, but was put on the backburner until recent advances in computer technology and algorithms gave researchers the necessary processing capability. And though some studies have taken advantage of the new tech to analyze a handful of smaller proteins and peptides, no group has analyzed a protein nearly as large as collagen – the subject of a new study by researchers at the University of Warwick (1). The researchers found that 2DMS could “uncoil collagen” two times faster than conventional methods.

“Collagen is a big protein, about 400 kDa, with many modified amino acids and crosslinks,” said Peter O'Connor, lead author of the study. “If we chop it into peptides using trypsin, and try to analyze the resulting mixture, there are thousands of peaks, and we can only assign a few dozen - the mixture is simply to complex.”