Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published February 1, 2019 | Supplemental Material
Journal Article Open

Replacement of ProB28 by pipecolic acid protects insulin against fibrillation and slows hexamer dissociation

Abstract

Non‐canonical amino acid mutagenesis was used to examine the biophysical consequences of changing ring size and structure at the single proline site in insulin. Addition of a methylene spacer to the prolyl ring (by replacement of proline by pipecolic acid at position B28) led to an increase in stability and a decrease in the rate of hexamer dissociation. The results of this work illustrate the power of non‐canonical amino acid mutagenesis in the engineering of macromolecular aggregation and protein therapeutics.

Additional Information

© 2018 Wiley Periodicals, Inc. Received 5 July 2018; Accepted 10 August 2018. K. Y. Fang and S. A. Lieblich contributed equally to this work. Funding Information: Amgen; Natural Sciences and Engineering Research Council of Canada (NSERC, PGS‐D); Natural Sciences and Engineering Research Council of Canada; Novo Nordisk Foundation.

Attached Files

Supplemental Material - pola29225-sup-0001-supinfo.pdf

Files

pola29225-sup-0001-supinfo.pdf
Files (1.1 MB)
Name Size Download all
md5:9be0aaf647dc9a7412ca6f0aeb8d7321
1.1 MB Preview Download

Additional details

Created:
August 22, 2023
Modified:
October 18, 2023