Synthesis and characterization of a chimeric peptide derived from fasciculin that inhibits acetylcholinesterase
✍ Scribed by Roberto J. Falkenstein; Germán G. Gornalusse; Dr Clara Peña
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 180 KB
- Volume
- 10
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.554
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✦ Synopsis
Abstract
Fasciculins are peptides isolated from mamba (Dendroaspis) venoms which exert their toxic action by inhibiting acetylcholinesterase (AChE). They contain a characteristic triple stranded antiparallel β‐sheet formed by residues 22–27, 34–39 and 48–53. A chimeric peptide named Fas‐C, encompassing most of these sequences was synthesized using SPPS/Boc‐chemistry and characterized chemically, structurally and functionally. Fas‐C has two disulfide bridges, formed sequentially using dual cysteine protection.
SDS‐PAGE patterns, HPLC profiles and MS proved the peptide identity. Circular dichroism indicated the presence of 13.6% and 41.6% of β‐sheet and β‐turn, respectively, comparable to values observed in the native toxin. An inhibitory effect on eel AChE was displayed by the peptide (K~i~71.6 ± 18.3 µ M), although not reaching the affinity level of the parent native toxin (K~i~ 0.3 nM). It is confirmed that the principal binding region of fasciculin to AChE resides within loop II. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.
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