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Current trends in peptide synthesis protocols have emerged as the most attractive domain in the field of pharma and medicine. Since most of the peptide/peptidomimetic-based molecules serve as potential candidates for many diseases, as they are bioavailable molecules.
We present the synthesis of bioactive peptides through TAGGING approach with the help of TAG-OH as a linker to the Nα-protected amino acid.
FRDEHKK and NKDRG are two peptides that possess antioxidant and antiproliferative activity, and their in-silico investigations reveal that they exhibit anticancer properties when bound to the AXL kinase and EGFR proteins.
This TAG method enables the easy isolation of peptides at each step as solids, and all the impurities were washed off by simple filtration. The method allows a bulk-scale preparation of the peptides without any difficulty, and hence the protocol is highly efficient for the production of peptides of therapeutic importance.
The two peptides FRDEHKK and NKDRG were isolated as fine solids with 82% and 85% yield and were characterized by NMR and MASS spectroscopy. In-silico studies reveal FRDEHKK and NKDRG peptides exhibit good affinity towards EGFR and AXL kinase.
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