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 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.
College of Pharmacy, Pusan National University , Busan 609-735, Republic of Korea.
Huayue
H
Li
Mingzhi
M
Su
Mark T
MT
Hamann
John J
JJ
Bowling
Hyung Sik
HS
Kim
Jee H
JH
Jung
D000595:Amino Acid Sequence; D000818:Animals; D002918:Chymotrypsin / Q000378:metabolism; D018360:Crystallography, X-Ray; D003553:Cystine / Q000737:chemistry*; D006801:Humans; D008386:Marine Biology; D008958:Models, Molecular; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010196:Pancreatic Elastase / Q000378:metabolism; D010434:Pepsin A / Q000378:metabolism; D010455:Peptides / Q000737:chemistry*; D011161:Porifera / Q000737:chemistry*; D011487:Protein Conformation; D013237:Stereoisomerism; D014357:Trypsin / Q000378:metabolism
D010455:Peptides; C000590251:asteropsin E; D003553:Cystine; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D014357:Trypsin; D010434:Pepsin A