Refolding of Aggregation-Prone ScFv Antibody Fragments Assisted by Hydrophobically Modified Poly(sodium acrylate) Derivatives

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Martin , N , Costa , N , Wien , F , Winnik , F M , Ortega , C , Herbet , A , Boquet , D & Tribet , C 2017 , ' Refolding of Aggregation-Prone ScFv Antibody Fragments Assisted by Hydrophobically Modified Poly(sodium acrylate) Derivatives ' , Macromolecular Bioscience , vol. 17 , no. 2 , 1600213 . https://doi.org/10.1002/mabi.201600213

Title: Refolding of Aggregation-Prone ScFv Antibody Fragments Assisted by Hydrophobically Modified Poly(sodium acrylate) Derivatives
Author: Martin, Nicolas; Costa, Narciso; Wien, Frank; Winnik, Francoise M.; Ortega, Celine; Herbet, Amaury; Boquet, Didier; Tribet, Christophe
Contributor organization: Department of Chemistry
Laboratory of Polymer Chemistry (-2016)
University of Helsinki
Faculty of Pharmacy
Drug Research Program
Polymers
Date: 2017-02
Language: eng
Number of pages: 12
Belongs to series: Macromolecular Bioscience
ISSN: 1616-5187
DOI: https://doi.org/10.1002/mabi.201600213
URI: http://hdl.handle.net/10138/308067
Abstract: ScFv antibody fragments are a promising alternative to full-length antibodies for both therapeutic and diagnosis applications. They can be overexpressed in bacteria, which enables easy large scale production. Since scFv are artificial constructs, they are poorly soluble and prone to aggregation, which makes them difficult to manipulate and to refold. Here, stabilization and refolding of scFv fragments from urea-unfolded solutions are reported based on the use of micromolar amounts of polymers playing the role of artificial chaperons. Using fluorescence correlation spectroscopy, the size and aggregation number of complexes of scFv with unmodified or hydrophobically modified poly(sodium acrylate) are determined. The evolution of the secondary structure along the refolding procedure, in the presence or absence of 0.4 m L-arginine at scFv:polymer
Subject: antibodies
chaperon-like polymers
fluorescence correlation spectroscopy
protein folding: synchrotron-radiation circular dichroism
SINGLE-CHAIN FV
POLY(ACRYLATE) DERIVATIVES
CIRCULAR-DICHROISM
PROTEIN
THERAPY
CANCER
CHAPERONE
AFFINITY
NANOPARTICLES
SPECTROSCOPY
1182 Biochemistry, cell and molecular biology
216 Materials engineering
Peer reviewed: Yes
Rights: cc_by_nc
Usage restriction: openAccess
Self-archived version: acceptedVersion


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