Abstract:
:NLP-12a and b have been identified as cholecystokinin/sulfakinin-like neuropeptides in the free-living nematode Caenorhabditis elegans. They are suggested to play an important role in the regulation of digestive enzyme secretion and fat storage. This study reports on the identification and characterization of an NLP-12-like peptide precursor gene in the rat parasitic nematode Strongyloides ratti. The S. ratti NLP-12 peptides are able to activate both C. elegans CKR-2 receptor isoforms in a dose-dependent way with affinities in the same nanomolar range as the native C. elegans NLP-12 peptides. The C-terminal RPLQFamide sequence motif of the NLP-12 peptides is perfectly conserved between free-living and parasitic nematodes. Based on systemic amino acid replacements the Arg-, Leu- and Phe- residues appear to be critical for high-affinity receptor binding. Finally, a SAR analysis revealed the essential pharmacophore in C. elegans NLP-12b to be the pentapeptide RPLQFamide.
journal_name
Peptidesjournal_title
Peptidesauthors
Peeters L,Janssen T,De Haes W,Beets I,Meelkop E,Grant W,Schoofs Ldoi
10.1016/j.peptides.2011.10.014subject
Has Abstractpub_date
2012-03-01 00:00:00pages
82-7issue
1eissn
0196-9781issn
1873-5169pii
S0196-9781(11)00421-9journal_volume
34pub_type
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