Small globular protein motif forms particulate hydrogel under various ph conditions

Jun Fang, Xiaoning Zhang, Yuguang Cai, Yinan Wei

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Biocompatible hydrogels have great potentials in biomedical and biotechnological applications. In the current study, we reported a new naturally occurring protein motif that formed a transparent hydrogel when heated to 90°C at a concentration as low as 0.4 mg/mL. The protein motif is the C-terminal soluble domain of an Escherichia coli inner membrane protein YajC (YajC-CT). We investigated the conformational change and self-assembly of the protein that lead to the formation of hydrogels using multiple methods. Atomic force microscopy studies of dilute gel samples revealed the presence of β-sheet-rich fibrils that were 2 to 3 nm in height and micrometers in length, which appeared to originate from homogeneous particles. On the basis of these observations, we proposed a three-step pathway of YajC-CT gelation. Hydrogels formed at different pH contained slightly different fibril structures. To our knowledge, this is the smallest hydrogel-forming globular protein module that has been characterized in detail. It may be useful as a model system in the elucidation of the mechanisms of protein fibrillation and gelation processes.

Original languageEnglish
Pages (from-to)1578-1584
Number of pages7
Issue number5
StatePublished - May 9 2011

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry


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