MOTS-c 40mg

Molecular structure

MOTS-c is a short peptide encoded by an open reading frame within the mitochondrial 12S ribosomal RNA region. Its classification reflects the genomic origin of its coding sequence.

The molecule contains a mixture of hydrophobic, polar, aromatic, and charged residues. Tryptophan, tyrosine, and phenylalanine provide aromatic side chains, while arginine and lysine contribute positive charge under typical aqueous conditions.

The distribution of these residues influences solvation and molecular interactions. As with other short peptides, a single static structure may not represent every conformation present in solution.

Physicochemical properties

Theoretical molecular mass can be calculated from the sequence and specified terminal groups. Actual analytical measurements may differ depending on the presence of counterions, modifications, or impurities.

The peptide's charge and solubility depend on pH and solvent composition. Its aromatic residues can participate in noncovalent interactions, but the presence of aromatic groups does not by itself establish a specific binding partner.

Biochemical mechanisms

MOTS-c has been investigated in connection with AMPK-related signaling and cellular energy regulation. AMPK is a protein kinase that responds to changes in cellular energy status.

An observed change in AMPK activity does not establish that MOTS-c directly binds AMPK. Direct molecular binding, upstream signaling, and downstream metabolic changes are distinct experimental questions.

Scientific evidence

Its sequence and mitochondrial-derived classification are established. The precise molecular interactions responsible for its reported biochemical effects remain less completely characterized.

This product is intended solely for laboratory research purposes and is not approved for human or animal use.