Tricine as a convenient scaffold for the synthesis of C-terminally branched collagen-model peptides |
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Authors: | Maciej J. Stawikowski Gregg B. Fields |
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Affiliation: | 1. Department of Chemistry and Biochemistry, Florida Atlantic University, 777 Glades Rd, Boca Raton, FL 33431, United States;2. The Scripps Research Institute/Scripps Florida, 130 Scripps Way, Jupiter, FL 33458, United States |
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Abstract: | A novel and convenient method for the synthesis of C-terminally branched collagen-model peptides has been achieved using tricine (N-[tris(hydroxymethyl)methyl]glycine) as a branching scaffold and 1,2-diaminoethane or 1,4-diaminobutane as a linker. The peptide sequence was incorporated directly onto the linker and scaffold during solid-phase synthesis without additional manipulations. The resulting branched triple-helical peptides exhibited comparable thermal stabilities to the parent, unbranched sequence, and served as substrates for matrix metalloproteinase-1 (MMP-1). The tricine-based branch reported herein represents the simplest synthetic scaffold for the convenient synthesis of covalently linked homomeric collagen-model triple-helical peptides. |
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Keywords: | Triple-helical peptide Collagen Matrix metalloproteinase Peptide synthesis |
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