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The hydrophobic face of GLP-1, formed by the conserved residues Phe 22 , Ile/Val 23 , Trp 25 , and Leu 26 , is responsible for interacting with the hydrophobic binding pocket in the ECD of GLP1R [37]

Growth monitoring involved aseptic sampling from the culture broth at predetermined intervals (initially at 2 and 4 h, then every 30 min from 4 to 9 h, and every 2 h from 9 to 24 h), followed by serial tenfold dilutions and plating on supplemented TSA

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Its extended amino acid sequence, along with specific substitutions such as -aminoisobutyric acid (Aib) residues, enhances structural stability and receptor interaction in controlled research environments