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A 16-amino acid hexadecapeptide with an N-terminal tyrosine modification requires rigorous analytical confirmation

The predicted binding mode of 1j indicates the C5-amino substituent forms hydrogen bonding interaction with the carboxylic backbone of the Ser201 residue and a hydrophobic bonding with the Ser213 residue unlike the NCA amide group that is in hydrogen bonding distance from with the NNMT Ser213 residue

Other researchers delving into this trial also noticed that the peptide may have interacted with VEGF and Transforming Growth Factor Beta 1 (TGF-1)