• 1. Synthesis and characterization of a photocleavable collagen-like peptide
  Alfredo Ornelas,Kaitlyn N. Williams,Kevin A. Hatch,Aurelio Paez,Angela C. Aguilar,Cameron C. Ellis,Nishat Tasnim,Supriyo Ray,Carl W. Dirk,Thomas Boland,Binata Joddar,Chunqiang Li,Katja Michael Org. Biomol. Chem. 2018 16 1000
• 2. Expanding the NMR toolkit for biological solids: oxygen-17 enriched Fmoc-amino acids
  Brittney A. Klein,Dylan G. Tkachuk,Victor V. Terskikh,Vladimir K. Michaelis New J. Chem. 2021 45 12384
• 3. Amino acid-linked porphyrin-nitroimidazole antibiotics targeting Porphyromonas gingivalis
  Simon A. Dingsdag,Benjamin C-M. Yap,Neil Hunter,Maxwell J. Crossley Org. Biomol. Chem. 2015 13 98
• 4. Amino acid-linked porphyrin-nitroimidazole antibiotics targeting Porphyromonas gingivalis
  Simon A. Dingsdag,Benjamin C-M. Yap,Neil Hunter,Maxwell J. Crossley Org. Biomol. Chem. 2015 13 98
• 5. Efficient synthesis of pentasubstituted pyrroles via intramolecular C-arylation
  Barbora Lemrová,Michal Maloň,Miroslav Soural Org. Biomol. Chem. 2022 20 3811

• Solvents and Organic Chemicals Organic Compounds Benzenoids Fluorenes Fluorenes
• Solvents and Organic Chemicals Organic Compounds Benzenoids Fluorenes
• Solvents and Organic Chemicals Organic Compounds Acids/Esters

Introduction to Fmoc-Pro-OH (CAS No 71989-31-6) in Modern Chemical Biology and Medicinal Chemistry

Fmoc-Pro-OH, with the chemical name N-(9-fluorenylmethoxycarbonyl)-L-proline, is a crucial intermediate in the synthesis of peptides and peptidomimetics. This compound, identified by its CAS No 71989-31-6, has garnered significant attention in the fields of chemical biology and medicinal chemistry due to its versatility and role in constructing complex peptide structures. The Fmoc (9-fluorenylmethoxycarbonyl) group, a protecting group for amino functions, enhances the stability and reactivity of the peptide backbone during synthesis, making Fmoc-Pro-OH an indispensable tool for researchers.

The utility of Fmoc-Pro-OH extends beyond its role as a building block in peptide synthesis. Its incorporation into peptide chains has been explored in various therapeutic applications, including enzyme inhibition, receptor binding studies, and the development of novel drug candidates. The proline residue itself is particularly interesting due to its unique conformational properties, which can influence the overall structure and function of the peptide. Recent studies have highlighted the importance of proline residues in stabilizing beta-turns and loops in protein structures, making Fmoc-Pro-OH a valuable component in designing bioactive peptides.

In the realm of medicinal chemistry, the use of Fmoc-Pro-OH has been instrumental in the development of peptidomimetics that mimic the biological activity of natural peptides but with improved pharmacokinetic properties. For instance, research has demonstrated that incorporating proline into peptide mimetics can enhance their resistance to enzymatic degradation, thereby prolonging their half-life in vivo. This has opened up new avenues for treating various diseases where natural peptides are limited by their short half-life or poor bioavailability.

Recent advancements in solid-phase peptide synthesis (SPPS) have further underscored the importance of high-quality intermediates like Fmoc-Pro-OH. The efficiency and yield of SPPS depend heavily on the purity and reactivity of each amino acid derivative used. The introduction of optimized synthetic routes for compounds such as Fmoc-Pro-OH has enabled researchers to achieve higher yields and purities, facilitating more complex and ambitious peptide projects. These improvements have been particularly beneficial in large-scale production settings where cost-effectiveness and reproducibility are critical.

The role of Fmoc-Pro-OH in drug discovery has also been augmented by its compatibility with various coupling reagents used in peptide synthesis. This flexibility allows for seamless integration into diverse synthetic strategies, enabling chemists to explore a wide range of structural modifications. For example, the use of coupling reagents like HATU (1-hydroxy-7-azabenzotriazole trihydrochloride) or HBTU (1-hydroxybenzotriazole-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate) ensures efficient formation of amide bonds between amino acids, including those derived from Fmoc-Pro-OH.

The application of computational methods and machine learning algorithms has further enhanced the utility of Fmoc-Pro-OH in medicinal chemistry. By predicting optimal reaction conditions and identifying potential side products, these tools have streamlined the synthesis process and reduced experimental trial-and-error. This integration of computational chemistry with traditional synthetic techniques has allowed for more rapid identification and optimization of lead compounds derived from peptides containing proline residues.

In conclusion, Fmoc-Pro-OH (CAS No 71989-31-6) represents a cornerstone in modern peptide synthesis and drug development. Its unique properties as a building block for peptides make it an invaluable asset for researchers aiming to design novel therapeutic agents. The ongoing exploration of its applications in chemical biology and medicinal chemistry continues to yield exciting advancements, underscoring its enduring significance in scientific research.

• 77284-32-3(Fmoc-L-norleucine)
• 105047-45-8(Fmoc-lys-OH)
• 101555-62-8(Fmoc-D-Pro-OH)
• 103478-58-6(Fmoc-D-N-Me-Val-OH)
• 103478-62-2(Fmoc-N-Me-Leu-OH)
• 103478-63-3(N-(((9H-Fluoren-9-yl)methoxy)carbonyl)-N-methyl-D-leucine)
• 84000-11-3(Fmoc-N-Me-Val-OH)
• 88050-17-3((2S,4R)-1-{[(9H-fluoren-9-yl)methoxy]carbonyl}-4-hydroxypyrrolidine-2-carboxylic acid)
• 71989-20-3(Fmoc-L-glutamine)
• 35661-60-0(Fmoc-L-Leu-OH)