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

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• 作者：Huayue Li ; Mingzhi Su ; Mark T. Hamann ; John J. Bowling ; Hyung Sik Kim ; Jee H. Jung
• 刊名：Journal of Natural Products
• 出版年：2014
• 出版时间：February 28, 2014
• 年：2014
• 卷：77
• 期：2
• 页码：304-310
• 全文大小：410K
• 年卷期：v.77,no.2(February 28, 2014)
• ISSN：1520-6025

文摘

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鈥揇, 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.