Adipotide (FTPP) (10mg)

Adipotide Peptide (FTPP)

Adipotide peptide, also known as FTPP (Fat-Targeted Proapoptotic Peptide), fat-targeted proapoptotic peptide, or proapoptotic peptide, has been widely researched and is posited by scientists to be a proapoptotic peptide that may contribute to cell apoptosis. Adipotide may act as a peptide targeting prohibitin, which is why it is also called “prohibitin-targeting peptide 1” (Prohibitin-TP01).

Current research is still exploring Adipotide’s potential in this area and its potential actions related to its targeting properties.⁽¹⁾ Prohibitins are natural proteins considered by scientists to regulate such functions as cell formation, metabolism, and inflammation.

Research teams initially considered Adipotide for its supposed potential to mitigate the action of cancer cells. Still, the peptide indicated it may have research potential for experiments investigating lipolysis and obesity mitigation, leaving the research pioneers “at a loss of words.”⁽²⁾ It was presumed that Adipotide might prevent blood supply to the cancer cells, resulting in cell death and malignant cell growth inhibition.

Upon further research, the scientists suggested that the peptide appeared to exhibit the same mechanism of action but on fat cells instead. This “proof of concept” study was an early-stage experiment suggesting that the peptide may have significant potential. Yet, the compound has to be studied further to understand its full potential and impact on cells.

Overview

Researchers isolated a naturally occurring peptide (sequence CKGGRAKDC) via phage display methodology and combined it with a proapoptotic sequence, forming the now-termed Adipotide compound. Adipotide is homologous to the peptide sequence found in the white adipose tissue. Owing to this development and characteristics, researchers suggest that the peptide may possibly target the prohibitin PHB1 found at the surface of the adipose tissue—possibly attaching and thereby damaging it, potentially causing a blood supply disruption to the adipocytes (fat cells).⁽¹⁾

Prohibitions are considered by scientists to act as a vascular marker of the fatty tissues, and adipotide may possibly be able to identify these markers and consequently induce apoptosis in these cells.⁽³⁾ Further, researchers speculate that Adipotide may interact not only with prohibitin but also another receptor called annexin A2 (ANX2) and thus potentially disrupt their role in supporting blood and fat supply to fat cells in white adipose tissue. Studies suggest that prohibitin and ANX2, when interacting in a complex with a fatty acid transporter called CD36, may facilitate the uptake of fatty acids by the endothelium and their subsequent transport into adipocytes.

One study suggested that there was a purported white adipose tissue hypotrophy in murine models lacking ANX2, despite apparently normal white adipose tissue vascularization, adipogenesis, and glucose metabolism.

This condition was potentially attributed to reduced fatty acid uptake by white adipose tissue endothelium and adipocytes. It was suggested that the efficiency of fatty acid transport relies on the interaction of ANX2 and prohibitin. This interaction was posited to be essential for mediating fatty acid transport from the endothelium to adipocytes. Additionally, it was noted that ANX2 and prohibitin form a complex with CD36, and this interaction is crucial for fatty acid transport.

Importantly, the colocalization of prohibitin and CD36 on the adipocyte surface was induced by extracellular fatty acids, suggesting a dynamic regulation of this protein complex in response to fatty acid levels.

The study posited that the biochemical interaction between ANX2 and prohibitin potentially regulates CD36-mediated fatty acid transport in white adipose tissue, unveiling a potential pathway that compounds like Adipotide might target.⁽⁴⁾ Consequently, Adipotide is posited to potentially burn the fat stored in these fat cells as fuel, according to researchers’ speculations.⁽²⁾

Based on early preclinical studies on monkeys, it was also suggested that following Adipotide presentation, the monkeys exhibited apparently reduced insulin resistance.⁽⁵⁾

Chemical Makeup

Molecular Formula: C₁₅₂H₂₅₂N₄₄O₄₂
Molecular Weight: 2611.41 g/mol
Other Known Titles: FTPP

Research and Clinical Studies

1.) Adipotide (FTPP) Initial Research

Adipotide Peptide, also known as FTPP (Fat-Targeted Proapoptotic Peptide), has undergone extensive research. Scientists posit that it acts as a proapoptotic peptide contributing to cell apoptosis. Adipotide targets prohibitin, which is why it also bears the name “prohibitin-targeting peptide 1” (Prohibitin-TP01). Current research explores Adipotide’s potential in this area and its targeting properties. Prohibitins, natural proteins, regulate functions such as cell formation, metabolism, and inflammation.

Researchers initially considered Adipotide for its potential to mitigate cancer cell action. However, the peptide showed promise for experiments investigating lipolysis and obesity mitigation, leaving research pioneers surprised. Scientists presumed that Adipotide might prevent blood supply to cancer cells, leading to cell death and inhibiting malignant cell growth. Further research suggested that the peptide exhibits a similar mechanism of action on fat cells instead. This early-stage “proof of concept” study indicated significant potential, but researchers must study the compound further to understand its full impact on cells.

Researchers isolated a naturally occurring peptide (sequence CKGGRAKDC) using phage display methodology and combined it with a proapoptotic sequence, forming the Adipotide compound. Adipotide resembles the peptide sequence found in white adipose tissue. Researchers suggest that the peptide targets the prohibitin PHB1 on the surface of adipose tissue, potentially damaging it and disrupting blood supply to adipocytes (fat cells).

Prohibitions serve as vascular markers of fatty tissues, and adipotide may identify these markers and induce apoptosis in these cells. Researchers speculate that Adipotide interacts with prohibitin and another receptor called annexin A2 (ANX2), potentially disrupting their role in supporting blood and fat supply to fat cells in white adipose tissue. Studies indicate that prohibitin and ANX2, when interacting with a fatty acid transporter called CD36, help the endothelium take up fatty acids and transport them into adipocytes. One study suggested that murine models lacking ANX2 exhibited white adipose tissue hypotrophy, despite normal vascularization, adipogenesis, and glucose metabolism.

Researchers attributed this condition to reduced fatty acid uptake by white adipose tissue endothelium and adipocytes. They posited that the efficiency of fatty acid transport relies on the interaction between ANX2 and prohibitin, which is essential for mediating fatty acid transport from the endothelium into adipocytes. Additionally, researchers noted that ANX2 and prohibitin form a complex with CD36, which is crucial for fatty acid transport. Importantly, extracellular fatty acids induced the colocalization of prohibitin and CD36 on the adipocyte surface, suggesting dynamic regulation of this protein complex in response to fatty acid levels.

The study posited that the biochemical interaction between ANX2 and prohibitin regulates CD36-mediated fatty acid transport in white adipose tissue, unveiling a potential pathway that compounds like Adipotide might target. Consequently, researchers speculate that Adipotide may burn the fat stored in these fat cells as fuel.

Based on early preclinical studies on monkeys, researchers suggested that after Adipotide administration, the monkeys exhibited reduced insulin resistance.

Adipotide peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.

References:

1. Thuaud, F., Ribeiro, N., Nebigil, C. G., & Désaubry, L. (2013). Prohibitin ligands in cell death and survival: mode of action and therapeutic potential. Chemistry & biology, 20(3), 316–331. https://doi.org/10.1016/j.chembiol.2013.02.006
2. Melissa H., Cancer treatment shows promise for rapid weight loss, Los Angeles Times, 10 Nov. 2011. https://www.latimes.com/local/la-xpm-2011-nov-10-la-he-drug-fat-loss-20111110-story.html
3. Kolonin, Mikhail G., et al. “Reversal of obesity by targeted ablation of adipose tissue.” Nature Medicine vol. 10,6 (2004): 625-32. https://pubmed.ncbi.nlm.nih.gov/15133506/
4. Salameh A, Daquinag AC, Staquicini DI, An Z, Hajjar KA, Pasqualini R, Arap W, Kolonin MG. The prohibitin/annexin 2 interaction regulates fatty acid transport in adipose tissue. JCI Insight. 2016 Jul 7;1(10):e86351. doi: 10.1172/jci.insight.86351. PMID: 27468426; PMCID: PMC4959783.
5. Barnhart, Kirstin F., et al. “A peptidomimetic Targeting White Fat Causes Weight Loss and Improved Insulin Resistance in Obese Monkeys.” Science translational medicine vol. 3, 108 (2011): 108ra112. doi:10.1126/scitranslmed. 3002621. https://pubmed.ncbi.nlm.nih.gov/22072637/
6. Staquicini, Fernanda I., et al. “Vascular ligand-receptor mapping by direct combinatorial selection in cancer patients.” Proceedings of the National Academy of Sciences of the United States of America vol. 108, no. 46 (2011): 18637-42. doi:10.1073/pnas.1114503108. https://pubmed.ncbi.nlm.nih.gov/22049339/
7. Kim, Dong-Hoon et al. “Rapid and weight-independent improvement of glucose tolerance induced by a peptide designed to elicit apoptosis in adipose tissue endothelium.” Diabetes vol. 61.9 (2012): 2299-310. doi:10.2337/db11-1579. https://pubmed.ncbi.nlm.nih.gov/22733798/
8. Kolonin, Mikhail G., et al. “Reversal of obesity by targeted ablation of adipose tissue.” Nature Medicine vol. 10,6 (2004): 625-32. doi:10.1038/nm1048. https://pubmed.ncbi.nlm.nih.gov/15133506/