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. 2019 Oct 21;9:15061. doi: 10.1038/s41598-019-51455-8

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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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2D representation of the L-phenylalanine scaffold depicting the SAR. The α-amino and the α-carboxyl groups are indicated by red spheres, and both the positions are sterically restrained. The aliphatic portion of the side chain is marked as α and β (grey spheres), and both the sites can tolerate modifications. The aromatic ring of the side chain is indicated by a violet sphere. The different positions on the aromatic ring are as follows: ortho (o) (R₁ and R₁’, grey spheres), meta (m) (R₂ and R₂’, green spheres) and para (p) (R₃, grey sphere). All positions on the aromatic ring can tolerate modifications and steric bulk. However, the meta positions (green spheres) have been shown critical for affinity.