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Macrocyclic design strategies for small, stable parallel beta-sheet scaffolds.

ABSTRACT: Pairs of short peptide strands can be induced to adopt an antiparallel beta-sheet secondary structure in aqueous solution via a macrocyclic constraint, as illustrated by many natural and designed peptides. We show that an analogous strategy is successful for creation of small units of parallel beta-sheet secondary structure in aqueous solution. Cyclization in this case requires nonpeptide segments for N-to-N and C-to-C interstrand linkage. Surprisingly, we find that only one of these segments needs to be preorganized.

SUBMITTER: Freire F

PROVIDER: S-EPMC2723809 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

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Macrocyclic design strategies for small, stable parallel beta-sheet scaffolds.

Freire Felix F Gellman Samuel H SH

Journal of the American Chemical Society 20090601 23

Pairs of short peptide strands can be induced to adopt an antiparallel beta-sheet secondary structure in aqueous solution via a macrocyclic constraint, as illustrated by many natural and designed peptides. We show that an analogous strategy is successful for creation of small units of parallel beta-sheet secondary structure in aqueous solution. Cyclization in this case requires nonpeptide segments for N-to-N and C-to-C interstrand linkage. Surprisingly, we find that only one of these segments ne ...[more]

PMID: 19456161

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