Modifications | The SARS-CoV-2 coronavirus invades host cells by binding the angiotensin converting enzyme 2 (ACE2) receptor on human cell surface through its viral spike protein (S). A helical peptide sequence (spike-binding peptide 1, SBP1) derived from the α1 helix of ACE2 peptidase domain (ACE2-PD) could bind to the SARS-CoV-2 coronavirus. The SBP1 peptide specifically binds SARS-CoV-2-RBD with low nanomolar affinity. A 23-mer peptide sequence (SBP1) was synthesized by LifeTein microwave peptide synthesis. The 23 residues selected from the ACE2 α1 helix sequence (SBP1: IEEQAKTFLDKFNHEAEDLFYQS) could be used as the SARS-CoV-2 spike protein binder. See full description about this spike protein binder here. |
Scientific Background | C-SBP1: Peptide binder to the SARS-CoV-2 spike protein is a 24-residue synthetic peptide with the sequence Cys-Ile-Glu-Glu-Gln-Ala-Lys-Thr-Phe-Leu-Asp-Lys-Phe-Asn-His-Glu-Ala-Glu-Asp-Leu-Phe-Tyr-Gln-Ser. an Ahx spacer separates the peptide from an attached label or affinity handle; C-terminal amidation removes the terminal carboxylate charge. The sequence contains 1 cysteine residue, providing potential thiol/disulfide chemistry when the thiol is available; contains 2 Asp and 4 Glu residues, contributing anionic character near neutral pH; contains 4 aromatic residues that can contribute to hydrophobic or aromatic interactions. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence. |
Experimental Notes | Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions. |
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