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The Total Chemical Synthesis of Monocyte Chemotactic Protein‐1 (MCP‐1)
Author(s) -
Brown Angus R.,
Covington Maryanne,
Newton Robert C.,
Ramage Robert,
Welch Patricia
Publication year - 1996
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.46.o
Subject(s) - chemistry , cysteine , residue (chemistry) , monocyte , chemokine , chemotaxis , thiol , stereochemistry , combinatorial chemistry , biochemistry , biology , receptor , immunology , enzyme
The affinity‐based N α ‐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‐con taining protein in the reduced state. Oxidative folding was then used to furnish the biologically active β‐chemokine MCP‐1.