The structure of proteoglycan aggregate determined by atomic force microscopy

Ming Long Yeh, Zong Ping Luo

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

Proteoglycan aggregate is the major extracellular matrix component in cartilage, comprising about 18% of the dry weight of hyaline cartilage. The proteoglycan aggregate is the major substance in cartilage which resists compression in the joint. The purpose of this study was to utilize the newly developed imaging technique, Atomic force Microscopy (AFM), to visualize the ultrastructure of proteoglycan aggregates. The proteoglycan aggregate molecules were imaged in air using the tapping mode of the AFM. The images illustrated the ultrastructure of the aggregates, especially the individual proteoglycan and the core hyaluronic acid. In addition to the length and width of each molecule, the height of the proteoglycan aggregates and the individual proteoglycans could be directly measured. The images of the ultrastructures of proteoglycan aggregates visualized from the AFM are comparable with those using conventional electron microscopy approaches. Nevertheless, the sample preparation for AFM imaging does not involve fixation, staining, coating, and other routine procedures required for traditional electron microscopy imaging. Thus, this technique could be a simple alternative approach for future analysis of proteoglycan aggregate and its assembly.

Original languageEnglish
Pages (from-to)273-276
Number of pages4
JournalScanning
Volume26
Issue number6
DOIs
Publication statusPublished - 2004

All Science Journal Classification (ASJC) codes

  • Atomic and Molecular Physics, and Optics
  • Instrumentation

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