In the evolving field of peptide chemistry, researchers frequently encounter short-chain building blocks that serve as the foundation for complex molecular architectures. Among these, the dipeptide phe-val stan Phe-Val - an overview ds out as a subject of significant interest. As an enthusiast who explores biochemical derivatives, I have found t Product Name:H-Val-Val-Phe-OH peptide; Molecular Formula: C19H29N3O ; Molecular Weight: 363.46 ; Sequence: VVF ; Three letter code: H-Val-Val-Phe-OH.Read more hat understanding the nuances of these amino acid pairs provides a clearer picture of how minimal sequences influence structural biology.
Chemical Identity and Molecular Characteristics
The dipeptide phe-val is composed of two essential amino acid residues: phenylalanine (Phe) and valine (Val). When these two are connected through a standard peptide bond, they form a compound with the molecular formula: C14H20N2O3. This specific arrangement is often represented by the linear formula: C6H5CH2CH(NH2)CONHCH(CH2C6H5)COOH, which highlights the hydrophobic nature of the side chains involved.
For those interested in the structural representation, the condensed structural formula of the dipeptide Phe-Val (FV) is a common academic exercise. It illustrates how the carboxyl group of one amino acid reacts with the amino group of another, releasing a water molecule in the process. With an average mass of 264.325, this molecule is a frequent reference point in studies involving dipeptides.
Self-Assembly and Structural Research
One of the most fascinating aspects of working with these compounds is observing self-assembling dipeptides using heterochiral Phe-Val and Val-Phe. Unlike longer protein chains, these short sequences— H-VAL-PHE-OH - (CAS 3918-92-1) - Peptides often categorized under Phe dipeptides—exhibit a unique ability to form nanostructures. My engagement with these materials has shown that the stacking interactions between the aromatic rings of phenylalanine are critical for the formation of stable supramolecular structures.
Whether we are discussing H-VAL-PHE-OH is a dipeptide or its isomer, the research community often compares these t The structure of l-Phe–l-Val with the atomic numbering o other variants like H-Val-Val-OH or the more complex H-Val-Val-Phe-OH peptide. Each sequence provides distinct physical properties, making them valuable for those studying peptide-based materials.
Contextualizing Phe and Val
To fully appreciate the role of Phe and Val, it is helpful to look at them as individual entities. Phenylalanine is an aromatic amino acid known for its role in hydrophobic interactions, while Valine is a branched-chain amino acid that contributes to the rigidity of the peptide backbone. When combined in Val Phe sequences, they create a hydrophobic motif that is often studied in the context of amyloid proteins or synthetic gelation agents.
It is important to distinguish these from other rela dipeptide phe-val Molecular formula: C14H20N2O3 ted compounds such as L-Leucyl-L-phenylalanine, a dipeptide, or even the dipeptide phe pro variations. While they share a similar classification as a dipeptide formed from the amino acids phenylalanine and valine, their biological and chemical behaviors differ significantly based on t by Z Shlomo·2015·Cited by 43—Nanotubes formed byPhe-Phe dipeptideswere found to be highly stable yet in order to generate hydrogels based on this motif, thedipeptidehad Read more he specific side-chain interactions.
Practical Observations
In my personal Stacking interactions by two Phe side chains stabilize and exploration of these materials, I have noted that the synthesis of L-Phe-L-Val requires precise control over protecting groups to ensure the correct orientation of the amide linkage. The literature frequently discusses the structural integrity of these molecules in the gas phase or as part of hydrogel matrices. These minimalist building blocks prove that even the simplest combinations of amino acids can lead to highly sophisticated, ordered systems.
By focusing on the molecular formula: C14H20N2O3, researchers can better track the consistency and purity of their samples during experiments. As the field of nanotechnology continues to utilize these building blocks, the study of Phe-Val remains a cornerstone for those looking to design smart, self-assembling materials. Through rigorous documentation and consistent experimental protocols, we continue to uncover the potential held within these elegant, short-chain structures.