Ac-RYYRWK-NH2

From WikiMD's Wellness Encyclopedia


Ac-RYYRWK-NH2 is a synthetic peptide with potential applications in biomedical research. This peptide is characterized by its specific sequence of amino acids and its acetylated N-terminus and amidated C-terminus, which can influence its biological activity and stability.

Structure and Composition[edit | edit source]

Ac-RYYRWK-NH2 is composed of the following amino acids:

  • Acetylated N-terminus (Ac-)
  • Arginine (R)
  • Tyrosine (Y)
  • Tyrosine (Y)
  • Arginine (R)
  • Tryptophan (W)
  • Lysine (K)
  • Amidated C-terminus (-NH2)

The acetylation of the N-terminus and amidation of the C-terminus are modifications that can enhance the peptide's resistance to enzymatic degradation, potentially increasing its half-life in biological systems.

Biological Activity[edit | edit source]

The specific sequence of Ac-RYYRWK-NH2 suggests that it may interact with certain biological targets, such as receptors or enzymes, due to the presence of aromatic and basic residues. The presence of tryptophan and tyrosine residues may allow for interactions with hydrophobic pockets or aromatic stacking interactions, while the basic residues arginine and lysine can form ionic interactions with negatively charged sites.

Applications in Research[edit | edit source]

Ac-RYYRWK-NH2 can be used in various research applications, including:

  • Receptor Binding Studies: Due to its specific sequence, this peptide may be used to study interactions with G-protein coupled receptors (GPCRs) or other receptor types.
  • Enzyme Inhibition or Activation: The peptide may act as an inhibitor or activator of specific enzymes, depending on its sequence and modifications.
  • Cell Signaling Pathways: Researchers may use Ac-RYYRWK-NH2 to investigate its effects on cell signaling pathways, particularly those involving tyrosine kinases or other signaling proteins.

Synthesis and Modifications[edit | edit source]

The synthesis of Ac-RYYRWK-NH2 is typically achieved through solid-phase peptide synthesis (SPPS), a method that allows for the sequential addition of protected amino acids to a growing peptide chain. The acetylation and amidation are introduced during the synthesis process to ensure the desired modifications are present in the final product.

Safety and Handling[edit | edit source]

As with all synthetic peptides, proper safety protocols should be followed when handling Ac-RYYRWK-NH2. This includes wearing appropriate personal protective equipment (PPE) and following guidelines for storage and disposal.

Also see[edit | edit source]



This peptide related article is a stub. You can help WikiMD by expanding it.

WikiMD
Navigation: Wellness - Encyclopedia - Health topics - Disease Index‏‎ - Drugs - World Directory - Gray's Anatomy - Keto diet - Recipes

Search WikiMD

Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD

WikiMD's Wellness Encyclopedia

Let Food Be Thy Medicine
Medicine Thy Food - Hippocrates

Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.

Contributors: Prab R. Tumpati, MD