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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 (Ki71.6 ± 18.3 μM), although not reaching the affinity level of the parent native toxin (Ki 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.

Registro:

Documento: Artículo
Título:Synthesis and characterization of a chimeric peptide derived from fasciculin that inhibits acetylcholinesterase
Autor:Falkenstein, R.J.; Gornalusse, G.G.; Peña, C.
Filiación:Inst. Quimica y Fisicoquimica Biol., Departamento de Quimica Biologica, Universidad de Buenos Aires, Junín 956, 1113 Buenos Aires, Argentina
Palabras clave:Acetylcholinesterase; AChE; Anticholinesterase activity; Fasciculin; acetylcholinesterase; chimeric protein; cysteine; fasciculin; snake venom; article; binding affinity; chemical analysis; circular dichroism; controlled study; disulfide bond; eel; enzyme inhibition; high performance liquid chromatography; mass spectrometry; nonhuman; peptide analysis; peptide synthesis; polyacrylamide gel electrophoresis; priority journal; protein function; protein isolation; protein structure; Acetylcholinesterase; Amino Acid Sequence; Cholinesterase Inhibitors; Chymotrypsin; Elapid Venoms; Molecular Sequence Data; Peptides; Protein Structure, Secondary; Serine Endopeptidases; Anguilliformes; Crocodylus niloticus; Dendroaspis
Año:2004
Volumen:10
Número:6
Página de inicio:342
Página de fin:349
DOI: http://dx.doi.org/10.1002/psc.554
Título revista:Journal of Peptide Science
Título revista abreviado:J. Pept. Sci.
ISSN:10752617
CODEN:JPSIE
CAS:acetylcholinesterase, 9000-81-1; cysteine, 4371-52-2, 52-89-1, 52-90-4; fasciculin, 86697-68-9; snake venom, 55230-69-8; Acetylcholinesterase, EC 3.1.1.7; Cholinesterase Inhibitors; Chymotrypsin, EC 3.4.21.1; Elapid Venoms; Fas-C chimeric peptide; fasciculin, 86697-68-9; Peptides; prolyl oligopeptidase, EC 3.4.21.26; Serine Endopeptidases, EC 3.4.21.-
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10752617_v10_n6_p342_Falkenstein

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Citas:

---------- APA ----------
Falkenstein, R.J., Gornalusse, G.G. & Peña, C. (2004) . Synthesis and characterization of a chimeric peptide derived from fasciculin that inhibits acetylcholinesterase. Journal of Peptide Science, 10(6), 342-349.
http://dx.doi.org/10.1002/psc.554
---------- CHICAGO ----------
Falkenstein, R.J., Gornalusse, G.G., Peña, C. "Synthesis and characterization of a chimeric peptide derived from fasciculin that inhibits acetylcholinesterase" . Journal of Peptide Science 10, no. 6 (2004) : 342-349.
http://dx.doi.org/10.1002/psc.554
---------- MLA ----------
Falkenstein, R.J., Gornalusse, G.G., Peña, C. "Synthesis and characterization of a chimeric peptide derived from fasciculin that inhibits acetylcholinesterase" . Journal of Peptide Science, vol. 10, no. 6, 2004, pp. 342-349.
http://dx.doi.org/10.1002/psc.554
---------- VANCOUVER ----------
Falkenstein, R.J., Gornalusse, G.G., Peña, C. Synthesis and characterization of a chimeric peptide derived from fasciculin that inhibits acetylcholinesterase. J. Pept. Sci. 2004;10(6):342-349.
http://dx.doi.org/10.1002/psc.554