title: The total chemical synthesis of monocyte chemotactic protein-1 (MCP-1).
abstract: The affinity-based N (alpha)-amino protecting group tetrabenzo[a,c,g,i]fluorenyl-17 methoxycarbonyl (Tbfmoc) has been utilized as a hydrophobic probe to allow the simple, quick and highly effective isolation of a 76 residue cysteine-containing protein (MCP-1). The base-labile Tbfmoc group can be removed under very mild conditions, which preserve the thiol-containing protein in the reduced state. Oxidative folding was then used to furnish the biologically active beta-chemokine MCP-1.
authors.affiliation: Department of Chemistry, University of Edinburgh, UK.
authors.forename: A R
authors.initials: AR
authors.lastname: Brown
authors.forename: M
authors.initials: M
authors.lastname: Covington
authors.forename: R C
authors.initials: RC
authors.lastname: Newton
authors.forename: R
authors.initials: R
authors.lastname: Ramage
authors.forename: P
authors.initials: P
authors.lastname: Welch
mesh_terms: D000595:Amino Acid Sequence; D018932:Chemokine CCL2 / Q000138:chemical synthesis* / Q000235:genetics / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D006801:Humans; D066298:In Vitro Techniques; D013058:Mass Spectrometry; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009000:Monocytes / Q000187:drug effects; D010449:Peptide Mapping
chemical_list: D018932:Chemokine CCL2