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CYCLO(-PRO-PRO-PHE-PHE-VAL-ILE-MET-LEU-ILE) is a cyclic peptide composed of the amino acids proline, phenylalanine, valine, isoleucine, methionine, and leucine. Peptides are short chains of amino acids, which are the building blocks of proteins, and they often play crucial roles in biological processes. This specific cyclic peptide may have potential applications in the medical or pharmaceutical fields due to its enhanced stability and bioavailability compared to linear peptides. The unique sequence of amino acids in this peptide could also confer specific biological activities or binding properties that warrant further investigation and development.

193139-41-2

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193139-41-2 Usage

Uses

Used in Pharmaceutical Development:
CYCLO(-PRO-PRO-PHE-PHE-VAL-ILE-MET-LEU-ILE) is used as a potential pharmaceutical agent for its enhanced stability and bioavailability compared to linear peptides. The cyclic structure of the peptide may provide improved resistance to degradation, allowing for better absorption and longer-lasting effects in the body.
Used in Drug Delivery Systems:
In the field of drug delivery, CYCLO(-PRO-PRO-PHE-PHE-VAL-ILE-MET-LEU-ILE) can be utilized as a carrier for therapeutic agents. Its cyclic nature may enable the development of novel drug delivery systems that can improve the targeting and release of drugs, enhancing their efficacy and reducing side effects.
Used in Medical Research:
CYCLO(-PRO-PRO-PHE-PHE-VAL-ILE-MET-LEU-ILE) is used as a subject of study in medical research to explore its specific biological activities or binding properties. Understanding the peptide's interactions with biological targets could lead to the discovery of new therapeutic applications or the development of diagnostic tools.
Used in Biochemical Analysis:
In the field of biochemical analysis, CYCLO(-PRO-PRO-PHE-PHE-VAL-ILE-MET-LEU-ILE) can be employed as a tool to investigate the mechanisms of protein-protein or protein-ligand interactions. Its unique sequence and cyclic structure may provide insights into the role of peptide conformation in biological processes.
Used in Peptide Synthesis:
CYCLO(-PRO-PRO-PHE-PHE-VAL-ILE-MET-LEU-ILE) can be used as a template for the development of new cyclic peptides with tailored properties. By modifying the amino acid sequence or introducing additional functional groups, researchers can create novel peptides with specific therapeutic or diagnostic applications.

Check Digit Verification of cas no

The CAS Registry Mumber 193139-41-2 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,9,3,1,3 and 9 respectively; the second part has 2 digits, 4 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 193139-41:
(8*1)+(7*9)+(6*3)+(5*1)+(4*3)+(3*9)+(2*4)+(1*1)=142
142 % 10 = 2
So 193139-41-2 is a valid CAS Registry Number.

193139-41-2Upstream product

193139-41-2Downstream Products

193139-41-2Relevant academic research and scientific papers

Site Covalent Modification of Methionyl Peptides for the Production of FRET Complexes

Jadhav, Pramodkumar D.,Shen, Jianheng,Sammynaiken, Ramaswami,Reaney, Martin J. T.

, p. 17023 - 17034 (2015)

Flax cyclic peptides (orbitides, linusorbs (LOs)) [1-8-NαC],[1-MetO2]-linusorb B1 ([MetO2]-LO1) and [1-9-NαC],[1-MetO2]-linusorb B2 ([MetO2]-LO2) are biologically active. These LOs lack active nuclei commonly used in peptide modification. We have developed reactions to activate methionine methyl sulphide to produce stable derivatives. In these reactions, LOs are converted to sulfonium intermediates and subsequently to derivatives containing active nuclei while preserving their fundamental structures. The reaction conditions preserved cyclic peptide fundamental structure and organic solvent solubility. [Met]-LO1 and [Met]-LO2 analogues containing activated groups (-CN, -COOEt, and -NH2) in the form of methionine, methionine (S)-oxide, and methionine (S,S)-dioxide amino acids were synthesized and characterized by LCMS and 1D and 2D NMR spectroscopy. Coumarin orbitide complexes produced in this manner bind Eu3+ yielding FRET compounds that absorb energy through coumarin antennae and emit photons at lanthanide wavelengths.

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