Solution structure of a sponge-derived cystine knot peptide and its notable stability
- Authors
- Li, H[Li, Huayue]; Su, M[Su, Mingzhi]; Hamann, T[Hamann, T.]; Bowling, JJ[Bowling, John J.]; Kim, HS[Kim, Hyung Sik]; Jung, JH[Jung, Jee H.]
- Issue Date
- 2014
- Citation
- Journal of Natural Products, v.77, no.2, pp.304 - 310
- Indexed
- SCIE
SCOPUS
- Journal Title
- Journal of Natural Products
- Volume
- 77
- Number
- 2
- Start Page
- 304
- End Page
- 310
- URI
- https://scholarworks.bwise.kr/skku/handle/2021.sw.skku/57093
- DOI
- 10.1021/np400899a
- ISSN
- 0163-3864
- 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. ? 2014 The American Chemical Society and American Society of Pharmacognosy.
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Collections - Pharmacy > Department of Pharmacy > 1. Journal Articles
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