H-Leu-Ser-Ser-Phe-Val-Arg-Ile-NH2 is an amidated peptide with mixed hydrophobic and polar residues that influence folding and recognition. Its structure supports studies on ligand orientation and motif-driven interactions. Researchers employ it to explore conformational stability in short bioactive chains. The molecule aids peptide-design investigations.
1. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs
3. Cationic cell-penetrating peptides are potent furin inhibitors
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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