Probing the Structural Diversities of Long α-Neurotoxins by Fluorescence Quenching Studies View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-02

AUTHORS

Long-sen Chang, Shinne-ren Lin, Jeh-jeng Wang, Chun-chang Chang

ABSTRACT

Trp fluorescence of Ophiophagus hannah neurotoxins (Oh-4, Oh-6A, Oh-7, and Oh-8) and Bungarus multicinctus α-bungarotoxin was quenched by acrylamide and iodide. Acrylamide quenching studies indicated that the degree of exposure of Trp residues in the neurotoxins followed the order Oh-8 > Oh-7 > Oh-6A > Oh-4 > α-bungarotoxin, as did the accessibility for iodide. These results reveal that the exposed degree of Trp residues and the microenvironment surrounding Trp residues in the neurotoxins differ, even though their Trp residues and positively charged residues are located at the same or homologous positions. In contrast to unfolded Oh-4, Oh-6A, Oh-7, and α-bungarotoxin, unfolding of Oh-8 by reduction and S-carboxymethylation caused a notable decrease in the susceptibility of their Trp residues for iodide. These observations support the view that the side chains of Trp residues and positively charged residues in their native structure do not point toward the same spatial positions. Computer models of the neurotoxins are in good agreement with this proposition. These results elucidate why the conserved Trp residues and cationic groups do not always play the same roles in the biological activities of the neurotoxins. More... »

PAGES

115-121

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1011025323192

DOI

http://dx.doi.org/10.1023/a:1011025323192

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020901269

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11563691


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