198701-52-9

Upstream product

• 67-56-1 methanol 
• 34702-59-5 2',3',4',5',6'-Pentafluoro-L-phenylalanine 
• 136207-26-6 (S)-2-((tert-butoxycarbonyl)amino)-3-(perfluorophenyl)propanoic acid 

Downstream Products

• 1026587-10-9 (S)-2-Isocyanato-3-pentafluorophenyl-propionic acid methyl ester 
• 1207604-17-8 C₂₉H₃₄BF₅N₄O₄ 
• 1207604-38-3 (S)-methyl 2-((S)-2-(tert-butoxycarbonylamino)-3-(perfluorophenyl)propanamido)-3-(perfluorophenyl)propanoate 
• 198701-48-3 (S)-3-Pentafluorophenyl-2-[3-(5-thioxo-4,5-dihydro-[1,3,4]thiadiazol-2-yl)-ureido]-propionic acid methyl ester 

Relevant academic research and scientific papers

Self-assembly of a tripeptide into a functional coating that resists fouling

This communication describes the self-assembly of a tripeptide into a functional coating that resists biofouling. Using this peptide-based coating we were able to prevent protein adsorption and interrupt biofilm formation. This coating can be applied on numerous substrates and therefore can serve in applications related to health care, marine and water treatment.

Stabilizing and destabilizing effects of phenylalanine → F 5-phenylalanine mutations on the folding of a small protein

We report a systematic evaluation of phenylalanine-to-pentafluorophenylalanine (Phe → F5-Phe) mutants for the 35-residue chicken villin headpiece subdomain (c-VHP), the hydrophobic core of which features a cluster of three Phe side chains (residues 6, 10, and 17). Phe → F5-Phe mutations are interesting because aryl-perfluoroaryl interactions of optimal geometry are intrinsically more favorable than aryl-aryl interactions and because perfluoroaryl units are more hydrophobic than are analogous aryl units. One mutant, Phe-10 → F5-Phe, provides enhanced tertiary structural stability relative to the native sequence. The other six mutants analyzed caused a decrease in stability. Copyright