MOTS-c is a short peptide encoded within the mitochondrial genome and has been described in the scientific literature as a member of the mitochondrial-derived peptide (MDP) class. Publications discussing MDPs describe these peptides in the context of mitochondrial signaling and inter-organelle communication within experimental systems.

Reports involving MOTS-c describe its identification in cellular compartments including mitochondria and the nucleus under defined experimental conditions. Observations of peptide localization and molecular interactions are limited to non-clinical research settings and are reported as descriptive findings within cellular and animal model studies.

All references to MOTS-c are confined to mechanistic and observational research contexts and do not extend beyond laboratory-based investigation.

MOTS-c Structure, De BQUB17-JHolguera – Trabajo propio, CC BY-SA 4.0
Source: Wikipedia

Sequence: Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg
Molecular Formula: C₁₀₁H₁₅₂N₂₈O₂₂S₂
Molecular Weight: 2174.64 g/mol
PubChem SID: 255386757
CAS Number: 1627580-64-6
Reported Synonyms: Mitochondrial open reading frame of the 12S rRNA-c, MT-RNR1

MOTS-c is a 16–amino acid peptide whose primary structure and molecular composition have been characterized in biochemical research sources. Structural descriptions are limited to physicochemical attributes and reported sequence information derived from non-clinical research references.

In the scientific literature, MOTS-c has been referenced in non-clinical research involving cellular assays and animal model studies. These publications describe experimental contexts in which molecular interactions, signaling components, and pathway-associated markers were observed and recorded.

Reported research contexts include examination of:

• Mitochondrial signaling-associated molecular components
• Nuclear translocation phenomena under experimental conditions
• AMPK-associated signaling elements
• Metabolic pathway–related molecular markers
• Gene expression patterns evaluated in cellular and animal models

All reported applications are confined to descriptive investigation within controlled laboratory research environments.

Mechanistic discussions in preclinical publications describe MOTS-c in relation to intracellular signaling pathways associated with energy-sensing and stress-responsive molecular networks, including components of the AMPK signaling framework.

Additional references describe experimental observations of MOTS-c localization to the nucleus under defined laboratory conditions, alongside reported associations with transcriptional regulation of nuclear-encoded genes. These descriptions are limited to molecular and biochemical observations within experimental systems.

All pathway-related descriptions are restricted to non-clinical research contexts and do not imply functional outcomes.

Preclinical studies cited in the scientific literature describe observations involving MOTS-c in cellular and animal model systems. Reported observations include measurements of signaling-associated proteins, metabolite profiles, and gene expression markers recorded under defined experimental conditions.

Additional publications describe associations between MOTS-c and molecular features observed in experimental models of metabolic stress and mitochondrial perturbation. All reported findings are restricted to the experimental systems employed.

MOTS-c is supplied as a research-grade peptide material. Identity and composition have been reported as characterized using analytical techniques commonly applied to peptide research materials, including chromatographic and mass spectrometric methods.

Handling, storage, and analytical verification parameters are determined by individual laboratories in accordance with internal research protocols.

The above literature was researched, edited and organized by Dr. Logan, M.D. Dr. Logan holds a doctorate degree from Case Western Reserve University School of Medicine and a B.S. in molecular biology.

Dr. Changhan David Lee, contributor to “MOTS-c: A novel mitochondrial-derived peptide regulating muscle and fat metabolism,” and “The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress,” is a researcher at the School of Gerontology at USC Leonard Davis.

Pinchas Cohen, MD, is the dean of the USC Leonard Davis School of Gerontology, executive director of the Ethel Percy Andrus Gerontology Center, and holder of the William and Sylvia Kugel Dean’s Chair in Gerontology. He is an expert in the study of mitochondrial peptides and their possible therapeutic benefits for diabetes, Alzheimer’s, and other diseases related to aging. Cohen’s current research focus is on the emerging science of mitochondria-derived peptides, which he discovered. These peptides include humanin, a 24-amino acid peptide encoded from the mt-16S-rRNA. It is a novel, centrally acting insulin sensitizer and metaboloprotective factor representing a new therapeutic and diagnostic target in diabetes and related disease. Other mitochondrial peptides of interest include MOTS-c, a second peptide encoded from a small ORF in the 12S region of the mitochondrial chromosome that has potent anti-diabetes and anti-obesity effect and acts as an exercise-mimetic, and SHLP2, a peptide encoded from the light strand of the mt-16S-rRNA region whose levels correlate with prostate cancer.

Dr. Changhan David Lee and Dr. Pinchas Cohen are being referenced as leading scientists involved in the research and development of Humanin. In no way are these doctors/scientists endorsing or advocating the purchase, sale, or use of this product for any reason. There is no affiliation or relationship, implied or otherwise, between Peptide Sciences and these doctors. The purpose of citing the doctors is to acknowledge, recognize, and credit the exhaustive research and development efforts conducted by the scientists studying this peptide. Dr. Changhan David Lee is listed in [1] [3] Dr. Pinchas Cohen is listed in [9] under the referenced citations.