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Solution structure of a sponge-derived cystine knot peptide and its notable stability.


ABSTRACT: A novel cystine knot peptide, asteropsin E (ASPE), was isolated from an Asteropus sp. marine sponge. The primary, secondary, and tertiary structures of ASPE were determined by high-resolution 2D NMR spectroscopy (900 MHz). With the exception of an N-terminal modification, ASPE shares properties with the previously reported asteropsins A-D, that is, the absence of basic residues, a highly acidic nature, conserved structurally important residues (including two cis-prolines), and a highly conserved tertiary structural framework. ASPE was found to be remarkably stable to gastrointestinal tract enzymes (chymotrypsin, elastase, pepsin, and trypsin) and to human plasma.

SUBMITTER: Li H 

PROVIDER: S-EPMC4128683 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

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Solution structure of a sponge-derived cystine knot peptide and its notable stability.

Li Huayue H   Su Mingzhi M   Hamann Mark T MT   Bowling John J JJ   Kim Hyung Sik HS   Jung Jee H JH  

Journal of natural products 20140205 2


A novel cystine knot peptide, asteropsin E (ASPE), was isolated from an Asteropus sp. marine sponge. The primary, secondary, and tertiary structures of ASPE were determined by high-resolution 2D NMR spectroscopy (900 MHz). With the exception of an N-terminal modification, ASPE shares properties with the previously reported asteropsins A-D, that is, the absence of basic residues, a highly acidic nature, conserved structurally important residues (including two cis-prolines), and a highly conserved  ...[more]

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