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Tricine as a convenient scaffold for the synthesis of C-terminally branched collagen-model peptides.

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.

SUBMITTER: Stawikowski MJ

PROVIDER: S-EPMC5846494 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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Tricine as a convenient scaffold for the synthesis of C-terminally branched collagen-model peptides.

Stawikowski Maciej J MJ Fields Gregg B GB

Tetrahedron letters 20171205 2

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 pare ...[more]

PMID: 29545652

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