Clustering of disulfide-rich peptides provides scaffolds for hit discovery by phage display: application to interleukin-23.

ABSTRACT:

Background

Disulfide-rich peptides (DRPs) are found throughout nature. They are suitable scaffolds for drug development due to their small cores, whose disulfide bonds impart extraordinary chemical and biological stability. A challenge in developing a DRP therapeutic is to engineer binding to a specific target. This challenge can be overcome by (i) sampling the large sequence space of a given scaffold through a phage display library and by (ii) panning multiple libraries encoding structurally distinct scaffolds. Here, we implement a protocol for defining these diverse scaffolds, based on clustering structurally defined DRPs according to their conformational similarity.

Results

We developed and applied a hierarchical clustering protocol based on DRP structural similarity, fol

SUBMITTER: Barkan DT 

PROVIDER: S-EPMC5120537 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature