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. 2023 Apr 19;15(1):2195517. doi: 10.1080/19420862.2023.2195517

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© 2023 The Author(s). Published with license by Taylor & Francis Group, LLC.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The terms on which this article has been published allow the posting of the Accepted Manuscript in a repository by the author(s) or with their consent.

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An SDS-PAGE image showing that stapled scFv (or spFv) runs faster than the unstapled scFv. DSC data indicate an approximately 12 °C increase in thermal stability (Tm) for these spFv molecules compared with the unstapled versions. — Stapling design improves the thermal stability of Cris7a/b domains. (a) SDS-PAGE of scFv and spFv proteins of Cris7a/Cris7b in LH orientation. (b) Thermal stability of Cris7a scFv/spFv and Cris7b scFv/spFv domains by DSC. Parameters related to protein design and enthalpy features from analysis are listed in Table S1.