## Background: Nuclease activity is thought to be a significant barrier to effective gene delivery employing synthetic vectors. in particular, the lysosomal dnase, dnase ii, has significant access to plasmid dna, when the protective condensing agent has been shed. here, we present the identificatio
Phage display screening for peptidic chitinase inhibitors
✍ Scribed by Cordula Petter; Christa Scholz; Helga Wessner; Gerd Hansen; Peter Henklein; Takeshi Watanabe; Wolfgang Höhne
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 420 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0952-3499
- DOI
- 10.1002/jmr.911
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
A phage display library with disulfide‐cyclized peptides was screened for peptides binding to chitinases from Serratia marcescens. One of those peptides was found to efficiently inhibit chitinase A and two others were inhibitors of chitinase B. Complete substitutional analysis of all three peptides using cellulose‐bound peptide spot synthesis revealed key interaction positions and allowed optimization of the chitinase B inhibitory peptides towards higher affinity, with inhibitory constants in the lower nanomolar range. Inhibition by all peptides proved to be competitive and highly specific for the chitinase used to select them, as shown with a series of chitinases from different organisms. Copyright © 2008 John Wiley & Sons, Ltd.
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