ArticleACS omega2018
Insights into the Folding of Disulfide-Rich μ-Conotoxins.
Article in ACS omega, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The trial behind it
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Who cites it
14 citing papers in PubMed.
- Article
- Chemical Synthesis and Insecticidal Activity Research Based on α-Conotoxins.Molecules (Basel, Switzerland) · 2024Article
- Review
- Inferring Pathways of Oxidative Folding from Prefolding Free Energy Landscapes of Disulfide-Rich Toxins.The journal of physical chemistry. B · 2023Article
- Host and viral proteins involved in SARS-CoV-2 infection differentially bind heme.Protein science : a publication of the Protein Society · 2022Article
- Article
- NMR-Based Structural Characterization of a Two-Disulfide-Bonded Analogue of the FXIIIa Inhibitor Tridegin: New Insights into Structure-Activity Relationships.International journal of molecular sciences · 2021Article
- Revisiting the Formation of a Native Disulfide Bond: Consequences for Protein Regeneration and Beyond.Molecules (Basel, Switzerland) · 2020Review
- Folding of Truncated Granulin Peptides.Biomolecules · 2020Article
- Graph-Directed Approach for Downselecting Toxins for Experimental Structure Determination.Marine drugs · 2020Article
- A Chemical Biology Approach to Probing the Folding Pathways of the Inhibitory Cystine Knot (ICK) Peptide ProTx-II.Frontiers in chemistry · 2020Article
- Effect of Conformational Diversity on the Bioactivity of µ-Conotoxin PIIIA Disulfide Isomers.Marine drugs · 2019Article
- Coagulation Factor XIIIa Inhibitor Tridegin: On the Role of Disulfide Bonds for Folding, Stability, and Function.Journal of medicinal chemistry · 2019Article
- Snails In Silico: A Review of Computational Studies on the Conopeptides.Marine drugs · 2019Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The study of protein conformations using molecular dynamics (MD) simulations has been in place for decades. A major contribution to the structural stability and native conformation of a protein is made by the primary sequence and disulfide bonds formed during the folding process. Here, we investigated μ-conotoxins GIIIA, KIIIA, PIIIA, SIIIA, and SmIIIA as model peptides possessing three disulfide bonds. Their NMR structures were used for MD simulations in a novel approach studying the conformations between the folded and the unfolded states by systematically breaking the distinct disulfide bonds and monitoring the conformational stability of the peptides. As an outcome, the use of a combination of the existing knowledge and results from the simulations to classify the studied peptides within the extreme models of disulfide folding pathways, namely the bovine pancreatic trypsin inhibitor pathway and the hirudin pathway, is demonstrated. Recommendations for the design and synthesis of cysteine-rich peptides with a reduced number of disulfide bonds conclude the study.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.