The total chemical synthesis of monocyte chemotactic protein-1 (MCP-1).
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.
Brown
A R
AR
Department of Chemistry, University of Edinburgh, UK.
Covington
M
M
Newton
R C
RC
Ramage
R
R
Welch
P
P
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
D018932:Chemokine CCL2