Anantin--a peptide antagonist of the atrial natriuretic factor (ANF). II. Determination of the primary sequence by NMR on the basis of proton assignments.
- Wyss DF Dept. of Organic Chemistry, University of Basel, Switzerland.
- Lahm HW
- Manneberg M
- Labhardt AM
- 1991-02-01
Published in:
- The Journal of antibiotics. - 1991
Amino Acid Sequence
Amino Acids
Atrial Natriuretic Factor
Chromatography, High Pressure Liquid
Magnetic Resonance Spectroscopy
Mass Spectrometry
Molecular Sequence Data
Peptides, Cyclic
English
Anantin, a naturally occurring peptide from Streptomyces coerulescens, binds competitively to the receptor of atrial natriuretic factor (ANF) from bovine adrenal cortex (Kd = 0.6 microM) and acts as ANF antagonist. Protein chemical data and FAB-MS have identified anantin to be a cyclic polypeptide consisting of 17 common L-amino acids. The molecule is highly stable and precludes the application of standard sequencing methods. The primary sequence of anantin was determined by 2D 1H NMR spectroscopy and the application of advanced protein chemical methods to be Gly1-Phe2-Ile3-Gly4-Trp5-Gly6-Asn7-Asp8 -Ile9-Phe10-Gly11-His12-Tyr13-Ser14+ ++- Gly15-Asp16-Phe17. The molecule is cyclized between the beta-carboxyl group of Asp8 and the amino group of Gly1.
- Language
-
- English
- Open access status
- bronze
- Identifiers
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- DOI 10.7164/antibiotics.44.172
- PMID 1826288
- Persistent URL
- https://susi.usi.ch/global/documents/272005
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