Source:http://linkedlifedata.com/resource/pubmed/id/10503247
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
1999-11-2
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| pubmed:abstractText |
Mammalian fertilization depends upon successful binding and fusion between the membranes of the spermatozoon and the oocyte. These processes are thought to be mediated by a series of protein-protein interactions in which sperm antigens known as fertilins are thought to play a key role. Using a recently developed fluorescence technique, the interactions of the oligopeptide sequence corresponding to the fusogenic domain of mouse fertilin-alpha (MF alpha P) and phospholipid vesicles have been investigated. Following stopped-flow mixing, MF alpha P bound rapidly to phospholipid membranes in a co-operative manner with a Hill coefficient of 2.4 and binding rate constants in excess of 1000 s-1. The co-operative nature of the binding process is suggested to represent evidence of a structural mechanism to prevent egg fertilization by immature spermatozoa. The subsequent membrane insertion was found to take place over a longer time period (with rate constants of up to 6.3 s-1), and was linear with respect to peptide concentration. Comparison of these processes with similar time-resolved circular dichroism measurements revealed that changes in peptide secondary structure were very rapid. Fourier transform infrared spectroscopy measurements confirmed changes in the secondary structure of MF alpha P during interaction with PC phospholipid membranes, indicating that the peptide is mainly present in a beta-structure with a small proportion of alpha-helix. These results are consistent with the hypothesis that fertilin-alpha is the fusogenic species with an important role in fertilization.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADAM Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescein,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylethanolamines,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/fertilin
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| pubmed:status |
MEDLINE
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| pubmed:issn |
0968-7688
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
16
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
257-63
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| pubmed:dateRevised |
2009-9-2
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| pubmed:meshHeading |
pubmed-meshheading:10503247-ADAM Proteins,
pubmed-meshheading:10503247-Amino Acid Sequence,
pubmed-meshheading:10503247-Animals,
pubmed-meshheading:10503247-Circular Dichroism,
pubmed-meshheading:10503247-Fertilization,
pubmed-meshheading:10503247-Fluorescein,
pubmed-meshheading:10503247-Lipid Bilayers,
pubmed-meshheading:10503247-Male,
pubmed-meshheading:10503247-Membrane Glycoproteins,
pubmed-meshheading:10503247-Metalloendopeptidases,
pubmed-meshheading:10503247-Mice,
pubmed-meshheading:10503247-Molecular Sequence Data,
pubmed-meshheading:10503247-Peptides,
pubmed-meshheading:10503247-Phosphatidylethanolamines,
pubmed-meshheading:10503247-Phospholipids,
pubmed-meshheading:10503247-Protein Conformation,
pubmed-meshheading:10503247-Protein Structure, Secondary,
pubmed-meshheading:10503247-Spermatozoa,
pubmed-meshheading:10503247-Time Factors
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| pubmed:articleTitle |
Membrane interactions of the putative fusion peptide (MF alpha P) from fertilin-alpha, the mouse sperm protein complex involved in fertilization.
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| pubmed:affiliation |
Institute of Food Research, Norwich Research Park, Colney, UK.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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