Pathway to insoluble aggregates on the refolding of a single-chain Fv antibody: Morphological changes of aggregated protein on refolding

Mitsuo Umetsu, Kumar Ashish, Kouhei Tsumoto, Izumi Kumagai

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

In vitro aggregated single-chain Fv antibody (scFv) was analyzed by attenuated total reflectance Fourier transform infrared spectra and scanning electron microscope images. The spectroscopic results demonstrate that the formation of β-strands is a first trigger to the off-pathway toward insoluble aggregates, which is independent of redox condition; however, the morphology of the insoluble aggregates is strongly influenced by the environment in which scFv is aggregated.

Original languageEnglish
Pages (from-to)1600-1601
Number of pages2
JournalChemistry Letters
Volume33
Issue number12
DOIs
Publication statusPublished - 2004 Dec 5

ASJC Scopus subject areas

  • Chemistry(all)

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