In the realm of bioch Lanreotide Categorised Product List emical research and synthetic biology, the lanreotide p Lanreotide acetate eptide sequence represents a fascinating study in molecular design. As a synthetic cyclic octapeptide analogue of somatostatin, lanreo by C Valéry·2008·Cited by 78—The lanreotide sequencecontains three aromatic amino acids in a total of eight. Besides these hydrophobic aromatic residues, it has two positive charges, which Read more tide has garnered significant interest for its unique structural properties and its ability to undergo self-assembly into nanotubes.
The Structural Architecture of Lanreotide
Lanreotide is a synthetic polypeptide analogue of somatostatin that mimics the native hormone's biological activity. Structurally, it is defined by its precise amino acid sequence, which consists of eight residues. Specifically, the peptide sequence is categorized as: D-Nal-Cys-Tyr-D-Trp-Lys-Val-Cys-Thr-NH2.
A critical feature of this molecule is the disulfide bridge that connects the two cysteine residues, locking the structure into a stable β-hairpin conformation. This LAN is a well-preorganized peptide scaffold, which is essential for its functional efficacy. Researchers often note that the molecule contains three aromatic amino acids in a total of eight, which contributes significantly to its hydrophobic core and its propensity for supramolecular organization.
Technical Parameters and Composition
When analyzing the lanreotide structure, it is helpful to look at its chemical classification. It is a peptide, specifically falling under the definition of molecules composed of between three and ten alpha-amino acids joined by peptide bonds.
* Chemical Formula: C54H69N11O10S2
* Molecular Weight: Approximately 1096.3 g/mol
* Key Characteristics: The sequence includes aliphatic side chains—one hydrophobic (Val) and one hydrophilic (Thr)—which, alongside its aromatic components, drive the self-assembly properties of specific amino acid sequences.
Research Context and Observations
In my personal experience reviewing analytical data regarding synthetic peptides, the distinction between lanreotide and related somatostatin analogues li Lanreotide | C54H69N11O10S2 | CID 6918011 - PubChem ke octreotide is often found in their cyclic backbones and specific side-chain configurations. While both are used in the management of acromegaly and are recognized as a class of artificially synthesized growth hormone inhibin analogues, the specific lanreotide peptide sequence is highly optimized for its controlled-release characteristics.
The study of these peptide sequences is paramount for understanding how small changes in the amino acid sequence can alter the stability or the self-assembly profile of the final product. For instance, altering a single amino acid's configuration within the chain can compromise the integrity of the scaffold, highlighting the importance of high-purity synthesis.
Summary of Findings
The LANREOTIDE molecule remains a corner Lanreotide | C54H69N11O10S2 | CID 6918011 - PubChem stone in peptide chemistry research. Its ability to form crystalline nanotubes through self-assembly is a direct result of its carefully balanced sequence, which facilitates the segregation of hydrophobic and hydrophilic regions. Whether one is investigating the molecular origins of these structures or exploring the synthesis of sequences for research purposes, the technical precision required for handling such an octapeptide used in the treatmen Primarily, peptides were synthesized using 448 mg (0.3 mmol, 0.67 mmol/g loading capacity) resin in a solid-phasepeptidesynthesis vessel. The synthetic route Read more t of acromegaly (in therapeutic contexts) is immense.
For those interested in identifying high-quality materials, there are many categorised Atomic structure of Lanreotide nanotubes revealed by cryo- products for chemical name Lanreotide available for laboratory use. Always ensure that the analytical documentation, such as HPLC or MS data, confirms the sequence integrity to avoid common issues like deletion sequences or incomplete peptide chains. Understanding the fundamental nature of this peptide allows researchers to better appreciate the complex supramolecular structures it can form under controlled experimental conditions.