Scientific Background | Peptide Z is a 132-residue synthetic peptide with the sequence Ala-Cys-Phe-Lys-Gly-Gly-Gly-Glu-Arg-Cys-Gly-Gly-Gly-Gly-Lys-Lys-Lys-Ala-Ala-Ala-Ala-Leu-Leu-Ala-Ala-Ala-Ala-Ala-Ala-Ala-Leu-Leu-Ala-Ala-Ala-Lys-Lys-Asn-His-Thr-His-Glu-Ile-Ser-Arg-Ile-Cys-His-Ile-Asn-Gly-Leu-Tyr-Cys-Ile-Asn-Glu-Ala-Asn-Asp-Ala-Leu-Ala-Asn-Ile-Asn-Glu-Trp-Ile-Thr-His-Ser-Thr-Arg-Glu-Thr-Cys-His-Glu-Ser-Leu-Tyr-Ser-Ile-Asn-Glu-Ile-Asn-Asp-Ile-Cys-Ala-Thr-Ile-Asn-Gly-Leu-Ile-Lys-Glu-Leu-Tyr-Ala-Asn-Asp-Ser-Glu-Glu-Asn-Ile-Asn-Leu-Ile-Asn-Lys-Glu-Arg-Ser-Leu-Ile-Lys-Glu-Leu-Tyr-Leu-Ile-Asn-Lys-Glu-Arg-Ile-Asn. C-terminal amidation removes the terminal carboxylate charge. The sequence contains 6 cysteine residues, which can support thiol-selective conjugation or disulfide chemistry when the thiol group is available; is enriched in basic residues (10 Lys and 5 Arg), giving the sequence a cationic character under many aqueous conditions; contains 6 aromatic residues (Phe/Trp/Tyr), which can contribute to hydrophobic or aromatic interactions. No specific receptor, enzyme, pathway, disease association, or biological activity is assigned to this peptide without product-specific experimental evidence. |
Experimental Notes | Sequence-derived chemical properties are provided to support reagent selection and experimental planning. They do not establish a biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions. |
