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1-naphthylpropargyl ether group: a readily cleaved and sterically minimal protecting system for stereoselective glycosylation.

ABSTRACT: [reaction: see text] The (1-naphthyl)propargyl group is introduced as a sterically unobtrusive alcohol protecting group that is cleaved in a single step by exposure to dichlorodicyanoquinone in wet dichloromethane. In conjunction with the 4,6-O-benzylidene protecting group, and the use of the sulfoxide glycosylation method, 3-O-naphthylpropargyl-protected mannosyl donors are extremely beta-selective.

SUBMITTER: Crich D

PROVIDER: S-EPMC2615467 | biostudies-literature | 2006 Oct

REPOSITORIES: biostudies-literature

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Publications

1-naphthylpropargyl ether group: a readily cleaved and sterically minimal protecting system for stereoselective glycosylation.

Crich David D Wu Baolin B

Organic letters 20061001 21

[reaction: see text] The (1-naphthyl)propargyl group is introduced as a sterically unobtrusive alcohol protecting group that is cleaved in a single step by exposure to dichlorodicyanoquinone in wet dichloromethane. In conjunction with the 4,6-O-benzylidene protecting group, and the use of the sulfoxide glycosylation method, 3-O-naphthylpropargyl-protected mannosyl donors are extremely beta-selective. ...[more]

PMID: 17020326

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Project description:Collagens and their most characteristic structural unit, the triple helix, play many critical roles in living systems which drive interest in preparing mimics of them. However, application of collagen mimetic helices is limited by poor thermal stability, slow rates of folding and poor equilibrium between monomer and trimer. Covalent capture of the self-assembled triple helix can solve these problems while preserving the native three-dimensional structure critical for biological function. Covalent capture takes advantage of strategically placed lysine and glutamate (or aspartate) residues which form stabilizing charge-pair interactions in the supramolecular helix and can subsequently be converted to isopeptide amide bonds under folded, aqueous conditions. While covalent capture is powerful, charge paired residues are frequently found in natural sequences which must be preserved to maintain biological function. Here we describe a minimal protecting group strategy to allow selective covalent capture of specific charge paired residues which leaves other charged residues unaltered. We investigate a series of side chain protecting groups for lysine and glutamate in model peptides for their ability to be deprotected easily and in high yield while maintaining (1) the solubility of the peptides in water, (2) the self-assembly and stability of the triple helix, and (3) the ability to covalently capture unprotected charge pairs. Optimized conditions are then illustrated in peptides derived from Pulmonary Surfactant protein A (SP-A). These covalently captured SP-A triple helices are found to have dramatically improved rates of folding and thermal stability while maintaining unmodified lysine-glutamate pairs in addition to other unmodified chemical functionality. The approach we illustrate allows for the covalent capture of collagen-like triple helices with virtually any sequence, composition or register. This dramatically broadens the utility of the covalent capture approach to the stabilization of biomimetic triple helices and thus also improves the utility of biomimetic collagens generally.

Dataset Information

1-naphthylpropargyl ether group: a readily cleaved and sterically minimal protecting system for stereoselective glycosylation.

Publications

1-naphthylpropargyl ether group: a readily cleaved and sterically minimal protecting system for stereoselective glycosylation.

Similar Datasets

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