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    Home > Biochemistry News > Biotechnology News > An Asymmetric Synthesis Protocol to Prepare Topographically Constrained -Substituted Aromatic Amino Acids

    An Asymmetric Synthesis Protocol to Prepare Topographically Constrained -Substituted Aromatic Amino Acids

    • Last Update: 2020-11-22
    • Source: Internet
    • Author: User
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    The side chain groups of amino acid residues in polypeptide hormones, neurotransmitters, growth factors, substrates, antigens, and other bioactive peptides have been demonstrated to be extremely important pharmacophores for receptor/acceptor binding and for signal transduction (
    1
    ). Therefore, complete understanding of the stereochemical requirements of side chain groups important in peptide ligand-receptor/acceptor interactions plays a crucial role in the rational design of bioactive peptides and nonpeptide mimetics. Topographical considerations provide a major approach to explore the structure–activity relationships of the side chains of the amino acid residues in the bioactive peptide analogues (
    2
    ). This approach can be realized by incorporation of conformationally constrained unusual amino acids into a peptide or nonpeptide template. Thus, design and synthesis of unusual amino acids with specific biased side chain conformations have tremendous impact on the exploration of the mechanism of peptide ligand-receptor recognition and of activating signal transduction. Our laboratory has been engaged in the design and synthesis of conformationally constrained amino acids for almost a decade. One representative family among the special amino acids we have designed is the β-substituted unusual amino acids, in which substitution of the diastereotopic β-hydrogens of natural α-amino acids provides an approach to topographic control of side chain conformation (
    3
    ). Incorporation of these β-substituted unusual amino acids into bioactive peptide hormones has produced highly selective and potent peptide hormone analogues and provided new insights into the stereochemical requirements in peptide-receptor interactions (
    4
    ).
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