Solution Structure of a Sponge-Derived Cystine Knot Peptide and Its Notable Stability

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...

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Bibliographic Details
Published in:Journal of natural products (Washington, D.C.) D.C.), 2014-02, Vol.77 (2), p.304-310
Main Authors: Li, Huayue, Su, Mingzhi, Hamann, Mark T, Bowling, John J, Kim, Hyung Sik, Jung, Jee H
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Asteropus
Chymotrypsin - metabolism
Crystallography, X-Ray
Cystine - chemistry
Humans
Marine Biology
Models, Molecular
Molecular Structure
Nuclear Magnetic Resonance, Biomolecular
Pancreatic Elastase - metabolism
Pepsin A - metabolism
Peptides - chemistry
Porifera - chemistry
Protein Conformation
Stereoisomerism
Trypsin - metabolism
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Summary: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.
ISSN:0163-3864
1520-6025
DOI:10.1021/np400899a