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. 2016 Aug 8;6:31295. doi: 10.1038/srep31295

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Copyright © 2016, The Author(s)

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(A) Peptides (Hx) derived from the VEGF helix (17-25). Hx peptide was acetylated at the N-terminus and amidated at the C-terminus. Hx was functionalized with a benzylthioester group on the side chain of Glu1. (B) Peptides (Hn) derived from the VEGF β-hairpin (79-93). Hn peptides differ for the length of the spacer. Hn peptides were amidated at the C-terminus. (C) Peptides obtained from the chemical ligation reaction between AcHx-thioester and the Hn peptides. EP number refers to the Hn peptide used. The chemical ligation reaction resulted in the formation of an isopeptide bond linking the carboxylic side chain of Hx Glu1 with Hn cysteine α-amino group. βAla = β-alanine; γAbu = γ-aminobutyric acid; 5Aval = 5-aminovaleric acid; εAhx = ε-aminocaproic acid; 7Ahp = 7- aminoheptanoic acid.