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

doi:10.1246/cl.2004.1600

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

ENG - Biomolecular Engineering

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	1600-1601
Number of pages	2
Journal	Chemistry Letters
Volume	33
Issue number	12
DOIs	https://doi.org/10.1246/cl.2004.1600
Publication status	Published - 2004 Dec 5

ASJC Scopus subject areas

Chemistry(all)

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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.",

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AU - Ashish, Kumar

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AU - Kumagai, Izumi

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AB - 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.

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

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