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Structure–activity relationships of peptidomimetics that inhibit PPI of HER2-HER3
Version of Record online: 25 MAR 2014
Copyright © 2013 Wiley Periodicals, Inc.
Volume 101, Issue 6, pages 693–702, June 2014
How to Cite
Kanthala, S., Gauthier, T. and Satyanarayanajois, S. (2014), Structure–activity relationships of peptidomimetics that inhibit PPI of HER2-HER3. Biopolymers, 101: 693–702. doi: 10.1002/bip.22441
- Issue online: 25 MAR 2014
- Version of Record online: 25 MAR 2014
- Accepted manuscript online: 12 NOV 2013 10:45PM EST
- Manuscript Accepted: 5 NOV 2013
- Manuscript Revised: 1 NOV 2013
- Manuscript Received: 1 AUG 2013
- National Institute of General Medical Sciences of the National Institutes of Health [Institutional Development Award (IDeA)] . Grant Number: 8P20GM103424
Additional Supporting Information may be found in the online version of this article.
Fig S1. Competitive binding assay for control compound (see Table 1 for structure). FITC-labeled compound 5 was incubated with different concentrations of control compound with BT-474 cells. Cells were washed with PBS and fluorescence was detected using a plate reader. Ex λ 485 nm, Em λ 535 nm. There was no difference in fluorescence observed by FITC-5 at different concentrations of control suggesting that binding was not observed.
Fig. S2. Structure of compound 19.
Fig. S3. Structure of compound 20.
Fig. S4. PathHunter assay for control compound (CP from Tables 1 and 2) in HER2-HER3-transfected U2OS cells at different concentrations. Dose-response curve for CP suggests that there was no inhibition of PPI of HER2:HER3 by the compound (filled triangles) in the presence 0.3 µM heregulin a HER2:HER3 dimerization inducer. For comparison induction of dimerization by heregulin in a dose dependent manner is also shown (filled circles).
Fig. S5. Docking of compound 21 to HER2 domain IV. Possible modes of docking of compound 21 are shown. Two clusters were observed.
Table S1. Docking energy and binding site of docked compounds to HER2 domain IV.
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