A New Method for Investigating Osteoarthritis using Fast Field Cycling Nuclear Magnetic Resonance

Lionel Broche, James Ross* (Corresponding Author), Brett Kennedy, Campbell MacEachern, David Lurie, George P. Ashcroft

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)
2 Downloads (Pure)


Human articular hyaline cartilage is composed of a dense extracellular matrix (ECM) made up of 70% water and 30% protein. The major protein components are type II collagen and proteoglycans, with other non-collagenous proteins present in small amounts. All are regenerated slowly but continuously by chondrocyte cells through the structure [1] and it is the combination of proteoglycans held within the overall collagen structure that combines to hold water in the ECM, which is essential in the maintenance of its unique mechanical properties. The interactions between proteoglycans and collagen are elusive but known to be of electrostatic nature [2].
Original languageEnglish
Pages (from-to)142-147
Number of pages6
JournalPhysica Medica
Early online date7 Jul 2021
Publication statusPublished - Aug 2021

Bibliographical note

We acknowledge ARUK (Versus Arthritis) for funding this study (grant number 19869) and the NHS Grampian Biorepository for the access to cartilage samples. BWCK received a Foulkes Foundation Fellowship. This project has also received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 668119 (project “IDentIFY”) and
NHS Grampian endowments. This work received support from the EURELAX COST Action CA15209, supported by COST (European Cooperation in Science and Technology).


  • Fast field-cycling NMR
  • Human hyaline cartilage
  • osteoarthritis
  • T1 dispersion
  • Quadrupolar peaks
  • protein interactions


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