Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Solution structure of alpha-conotoxin SI.

A J Benie¹, D Whitford, B Hargittai

¹Molecular and Cellular Biology, St. Bartholomew's and the Royal London School of Medicine and Dentistry, University of London, UK.

|July 29, 2000

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The Use of Arteriovenous Fistulae as an Adjunct to Peripheral Arterial Bypass: A Systematic Review and Meta-analysis.

European journal of vascular and endovascular surgery : the official journal of the European Society for Vascular Surgery·2016

Same author

New clustering methods for population comparison on paternal lineages.

Molecular genetics and genomics : MGG·2014

Same author

Facile solid-phase synthesis of C-terminal peptide aldehydes and hydroxamates from a common Backbone Amide-Linked (BAL) intermediate.

The journal of peptide research : official journal of the American Peptide Society·2005

Same author

Evaluation of geranylazide and farnesylazide diphosphate for incorporation of prenylazides into a CAAX box-containing peptide using protein farnesyltransferase.

The journal of peptide research : official journal of the American Peptide Society·2005

Same author

Preparation of protected peptidyl thioester intermediates for native chemical ligation by Nalpha-9-fluorenylmethoxycarbonyl (Fmoc) chemistry: considerations of side-chain and backbone anchoring strategies, and compatible protection for N-terminal cysteine.

The journal of peptide research : official journal of the American Peptide Society·2005

Same author

Facile preparation of disulfide-bridged peptides using the polymer-supported oxidant CLEAR-OX.

The journal of peptide research : official journal of the American Peptide Society·2004

Nuclear magnetic resonance revealed alpha-conotoxin SI has a stable structure. Differences in toxicity between alpha-conotoxin SI and GI are due to charge, not conformation changes.

Area of Science:

Biochemistry
Structural Biology
Neuroscience

Background:

Alpha-conotoxins are peptides found in cone snail venom.
These peptides are known for their potent neurotoxic effects.
Understanding their structure-activity relationship is crucial for drug discovery.

Purpose of the Study:

To determine the solution structure of alpha-conotoxin SI using nuclear magnetic resonance (NMR).
To compare the solution structure of SI with the known structures of alpha-conotoxin GI.
To elucidate the structural basis for the differential toxicity between SI and GI.

Main Methods:

Nuclear magnetic resonance (NMR) spectroscopy was used to determine the three-dimensional structure of alpha-conotoxin SI in solution.
Computational methods were employed to calculate the 36 lowest energy structures.

Related Experiment Videos

Structural comparisons were made between alpha-conotoxin SI and alpha-conotoxin GI.

Main Results:

Alpha-conotoxin SI adopts a single, stable solution conformation.
The structure is stabilized by six hydrogen bonds.
A high degree of backbone conformational similarity was observed between SI and GI, particularly in residues Gly-8 to Ser-12, despite sequence differences.
This similarity persisted even with a proline substitution for arginine at position 9 in SI compared to GI.

Conclusions:

The solution structure of alpha-conotoxin SI is well-defined and stable.
The conformational similarity between SI and GI suggests that structural changes are not the primary driver of toxicity differences.
The loss of the basic charge from arginine at residue 9 in SI is the key determinant of its altered toxicity compared to GI.