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. 2019 Feb 25;9:2723. doi: 10.1038/s41598-019-38574-y

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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(a) Chemical structure of peptide 1 (GE11) and peptide analogue 22. (b) Amino acid sequence of 53-mer human EGF (hEGF) and 12-mer 22 showing sequence homology for the G, Y and E residues (highlighted in red). Peptide 22 also shows structural similarity (based on secondary structure prediction of 22) to this cyclic region of hEGF (residues 32–43). (c) Predicted secondary structure of peptide 22 using Chou and Fasman secondary structure prediction (CFSSP) server^37,38. (d) 3D structure of a portion (residues 32–43) of hEGF derived from the crystal structure of full length hEGF (PDB code 1JL9)³⁵. (e) Energy minimized structure of peptide 22 obtained using PEP-fold 2.0⁴³ and Swiss-Pdb Viewer 4.1⁴². Side chains are not shown here for clarity.