When scientists changed two specific letters in the MOTS-c peptide, it stopped working—proving those spots are essential for its sugar-burning effect.
Scientific Claim
In HEK293 cells, substitution of two conserved residues (E5A and G7A) in MOTS-c abolished its ability to enhance glycolysis, indicating that these amino acids are critical for its biological activity.
Original Statement
“We substituted 2 highly conserved residues to alanine and created null mutants that did not show enhanced glycolytic response to glucose stimulation in HEK293 cells. These mutants were glutamic acid in position 5 (E5A) and glycine in position 7 (G7A)...”
Evidence Quality Assessment
Claim Status
appropriately stated
Study Design Support
Design supports claim
Appropriate Language Strength
association
Can only show association/correlation
Assessment Explanation
The study demonstrates loss-of-function via mutagenesis in a controlled cell model. The language appropriately reflects association within the experimental context.
More Accurate Statement
“In HEK293 cells, substitution of two conserved residues (E5A and G7A) in MOTS-c was associated with abolition of its ability to enhance glycolysis, indicating that these amino acids are critical for its biological activity.”
Evidence from Studies
Supporting (0)
Contradicting (1)
The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance
This study talks about a mitochondrial peptide that helps regulate metabolism, but it doesn’t test whether changing two specific letters in the peptide breaks its function, so we can’t say if the claim is right or wrong.