Ac-Leu-Pro-Phe-Phe-Asp--NH2 presents a hydrophobic core flanked by a terminal amide, contributing to defined secondary structure tendencies. The sequence architecture allows examination of protease recognition and peptide-receptor interactions. Its proline residue introduces conformational constraints valuable in folding studies. Applications extend to peptide design, biochemical mapping, and mechanistic enzymology.
CAT No: A13351
2. Immune-awakening Saccharomyces-inspired nanocarrier for oral target delivery to lymph and tumors
3. C-Peptide replacement therapy and sensory nerve function in type 1 diabetic neuropathy
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