Phe-Ile pairs an aromatic phenylalanine with hydrophobic isoleucine, forming a dipeptide ideal for studying π-stacking and side-chain packing. The sequence reveals valuable information about hydrophobic clustering in early folding events. Researchers analyze its conformational preferences across environments. Uses include synthetic method refinement, structural modeling, and binding studies.
CAT No: R2659
CAS No:22951-94-6
Synonyms/Alias:H-Phe-Ile-OH;Phe-Ile;22951-94-6;phenylalanylisoleucine;L-PHENYLALANYL-L-ISOLEUCINE;FI dipeptide;F-I Dipeptide;Phenylalanyl-Isoleucine;(2S,3S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-3-methylpentanoic acid;CHEBI:74717;Phenylalanine Isoleucine dipeptide;Phenylalanine-Isoleucine dipeptide;(2S,3S)-2-((S)-2-Amino-3-phenylPropanamido)-3-methylpentanoic acid;(2S,3S)-2-(((2S)-2-amino-3-phenylpropanoyl)amino)-3-methylpentanoic acid;(2S,3S)-2-(((2S)-2-azaniumyl-3-phenylpropanoyl)amino)-3-methylpentanoate;(2S,3S)-2-[[(2S)-2-azaniumyl-3-phenylpropanoyl]amino]-3-methylpentanoate;MFCD00038573;L-Phe-L-Ile;N-Phenylalanylisoleucine;N-L-Phenylalanyl-L-isoleucine;L-Isoleucine, L-phenylalanyl-;SCHEMBL3052110;FI;HY-P4473;AKOS010420075;FP108144;CS-0654413;Q27144854;
Phe-Ile, also known as Phenylalanyl-Isoleucine, is a synthetic dipeptide composed of the amino acids phenylalanine and isoleucine linked by a peptide bond. This compound is valued in biochemical research for its well-defined structure and stability, making it a useful model for investigating peptide behavior and interactions. Its amphipathic nature, arising from the hydrophobic side chains of both constituent amino acids, allows it to participate in a variety of experimental settings, ranging from enzymatic studies to structural analyses. Researchers often select Phe-Ile for its ability to mimic certain natural peptide sequences, thus providing insight into protein folding, substrate specificity, and molecular recognition processes. The dipeptide's manageable size and ease of synthesis further enhance its utility across diverse scientific disciplines, supporting both fundamental and applied research efforts.
Peptide Structure-Activity Relationship Studies: Phe-Ile serves as an important tool in structure-activity relationship (SAR) investigations, where scientists analyze how specific amino acid sequences influence biological activity. By incorporating this dipeptide into larger peptide frameworks or testing it as a standalone entity, researchers can assess how the sequence impacts receptor binding, enzymatic cleavage, or conformational stability. Such studies contribute to a deeper understanding of protein engineering and the rational design of bioactive peptides, guiding the development of molecules with tailored functionalities for use in research or industrial applications.
Protease Substrate Profiling: In enzymology, Phenylalanyl-Isoleucine is frequently employed as a model substrate for protease activity assays. Its defined sequence allows for precise evaluation of protease specificity, enabling the characterization of cleavage preferences and catalytic mechanisms. The dipeptide's susceptibility or resistance to various proteolytic enzymes provides valuable data for mapping active sites and understanding enzyme-substrate interactions. This information is crucial for designing selective inhibitors, optimizing biocatalysts, and elucidating the roles of proteases in physiological and pathological processes.
Peptide Transport and Absorption Research: The study of peptide transporters and absorption mechanisms in biological membranes often utilizes Phe-Ile as a representative dipeptide. Its physicochemical properties and manageable size make it suitable for investigating how peptides are recognized and transported by specific membrane proteins, such as PEPT1 and PEPT2. These experiments yield insights into nutrient uptake, drug delivery strategies, and the molecular basis of transporter selectivity. By tracing the movement and metabolism of this compound in model systems, researchers can advance the understanding of peptide pharmacokinetics and the optimization of orally bioavailable therapeutics.
Protein Folding and Aggregation Studies: Phenylalanyl-Isoleucine is also utilized in research focused on protein folding and aggregation phenomena. Its hydrophobic nature makes it relevant for modeling the interactions that drive peptide self-assembly, aggregation, or amyloid formation. By observing the behavior of this dipeptide under various conditions, scientists can uncover factors that influence folding pathways, stabilize native conformations, or promote aggregation. Such studies are instrumental in deciphering the molecular basis of protein misfolding disorders and in designing strategies to modulate aggregation for therapeutic or material science purposes.
Peptide-Based Material Science: In the field of material science, Phe-Ile finds application in the development of peptide-based nanomaterials and hydrogels. Its propensity to engage in hydrophobic interactions and self-assembly processes is harnessed to create novel biomaterials with tunable mechanical and functional properties. These materials can serve as scaffolds for tissue engineering, vehicles for controlled release, or components of biosensors. By manipulating the sequence and environmental conditions, researchers can fine-tune the assembly behavior and material characteristics, paving the way for innovative applications in biotechnology and regenerative medicine.
2. Low bone turnover and low BMD in Down syndrome: effect of intermittent PTH treatment
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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