Understanding the Benefits of Aib Residue in Peptide Synthesis with Fmoc-Ile-Aib-OH
At NINGBO INNO PHARMCHEM CO.,LTD., we specialize in providing essential components for cutting-edge scientific research. Fmoc-Ile-Aib-OH is a prime example of a chemical that significantly advances the field of peptide synthesis. A key feature of this compound is the alpha-aminoisobutyric acid (Aib) residue, a non-proteinogenic amino acid known for its unique structural properties. The inclusion of Aib via Fmoc-Ile-Aib-OH can dramatically influence the conformation and stability of peptides, making it a sought-after component for researchers exploring peptide backbone modifications and stability. For those needing to purchase Fmoc-Ile-Aib-OH, our commitment to quality ensures you receive a product that meets rigorous standards.
The structural impact of the Aib residue is well-documented in peptide chemistry. Unlike typical alpha-amino acids, Aib has two methyl groups attached to the alpha-carbon, preventing it from forming peptide bonds in the usual L or D configurations. This steric hindrance restricts the rotation around the peptide bond, favoring specific secondary structures, most notably the 310-helix and the alpha-helix. The formation of these stable helical structures can protect the peptide from proteolytic degradation, thereby increasing its in vivo half-life. This is a critical consideration for pharmaceutical building blocks for peptide drugs, as improved stability directly translates to better therapeutic efficacy and potentially less frequent dosing. When scientists are searching for Fmoc protected amino acids for SPPS, the unique properties of Aib are a major draw.
Furthermore, the incorporation of Aib residues can enhance the cell permeability of peptides. By adopting a more rigid, helical conformation, peptides may interact differently with cell membranes, facilitating their entry. This is particularly important for peptides that need to reach intracellular targets to exert their therapeutic effect. The precise control offered by using Fmoc-Ile-Aib-OH allows researchers to strategically introduce Aib at specific positions within a peptide sequence to fine-tune these properties. This level of customization is what makes it such a valuable tool for chemists developing new research chemicals for life sciences.
The synthesis of complex peptides often requires specialized building blocks that can overcome common challenges. The steric bulk of Aib, while beneficial for structure, can sometimes present coupling challenges in SPPS. However, Fmoc-Ile-Aib-OH is prepared and supplied in a form optimized for efficient coupling, ensuring that researchers can readily integrate this beneficial residue into their peptide designs. The availability of Fmoc-Ile-Aib-OH in various quantities, from research-scale grams to bulk kilograms, supports projects at every stage of development. NINGBO INNO PHARMCHEM CO.,LTD. is dedicated to supporting your research by providing high-purity Fmoc-Ile-Aib-OH price competitive and readily available.
In conclusion, the Aib residue, effectively delivered through Fmoc-Ile-Aib-OH, offers a distinct advantage in peptide synthesis by promoting stable secondary structures and potentially improving cell permeability. As a leading supplier of specialty amino acid derivatives, NINGBO INNO PHARMCHEM CO.,LTD. is proud to facilitate groundbreaking research by providing this essential compound.
Perspectives & Insights
Data Seeker X
“Unlike typical alpha-amino acids, Aib has two methyl groups attached to the alpha-carbon, preventing it from forming peptide bonds in the usual L or D configurations.”
Chem Reader AI
“This steric hindrance restricts the rotation around the peptide bond, favoring specific secondary structures, most notably the 310-helix and the alpha-helix.”
Agile Vision 2025
“The formation of these stable helical structures can protect the peptide from proteolytic degradation, thereby increasing its in vivo half-life.”