Document Detail

beta-Sheet aggregation of kisspeptin-10 is stimulated by heparin but inhibited by amphiphiles.
MedLine Citation:
PMID:  20301214     Owner:  NLM     Status:  MEDLINE    
The murine 10-residue neurohormone kisspeptin (YNWNSFGLRY) is an important regulator of reproductive behavior and gonadotrophin secretion. It is known to form a random coil in solution, but undergoes a structural change in the presence of membranes although the nature of this change is not fully determined. The peptide's conformational versatility raises the question whether it is also able to form ordered aggregates under physiological conditions, which might be relevant as a storage mechanism. Here we show that heparin induces kisspeptin to form beta-sheet rich amyloid aggregates both at neutral (pH 7.0) and slightly acidic (pH 5.2) conditions. Addition of heparin leads to aggregation after a certain lag phase, irrespective of the time of addition of heparin, indicating that heparin is needed to facilitate the formation of fibrillation nuclei. Aggregation is completely inhibited by submicellar concentrations of zwitterionic and anionic surfactants. Unlike previous reports, our NMR data do not indicate persistent structure in the presence of zwitterionic surfactant micelles. Thus kisspeptin can aggregate under physiologically relevant conditions provided heparin is present, but the process is highly sensitive to the presence of amphiphiles, highlighting the very dynamic nature of the peptide conformation and suggesting that kisspeptin aggregation is a biologically regulatable process.
Søren B Nielsen; Magnus Franzmann; Rajiv V Basaiawmoit; Reinhard Wimmer; Jens D Mikkelsen; Daniel E Otzen
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biopolymers     Volume:  93     ISSN:  0006-3525     ISO Abbreviation:  Biopolymers     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-06-02     Completed Date:  2010-08-19     Revised Date:  2010-12-09    
Medline Journal Info:
Nlm Unique ID:  0372525     Medline TA:  Biopolymers     Country:  United States    
Other Details:
Languages:  eng     Pagination:  678-89     Citation Subset:  IM    
Department of Molecular Biology, Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.
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MeSH Terms
Amino Acid Sequence
Circular Dichroism
Fluorescent Dyes
Heparin / pharmacology
Hydrogen-Ion Concentration
Microscopy, Atomic Force
Oligopeptides / chemistry*,  drug effects
Protein Multimerization / drug effects
Protein Structure, Secondary
Spectrometry, Fluorescence
Spectroscopy, Fourier Transform Infrared
Surface-Active Agents / pharmacology
Reg. No./Substance:
0/Fluorescent Dyes; 0/KISS1 protein, human; 0/Micelles; 0/Oligopeptides; 0/Surface-Active Agents; 0/Thiazoles; 2390-54-7/thioflavin T; 9005-49-6/Heparin

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