158641-77-1

Upstream product

• 2419-56-9 L-glutamic acid 5-tert-butyl ester 
• 42855-00-5 nitroveratryloxycarbonyl chloride 

Downstream Products

• 1209481-12-8 C₂₅H₂₅F₅N₂O₁₀ 

Relevant academic research and scientific papers

Automated maskless photolithography system for peptide microarray synthesis on a chip

Maskless photolithographic peptide synthesis was performed on a glass chip using an automated peptide array synthesizer system. The peptide array synthesizer was built in a closed box, which contained optical and fluidic systems. The conditions for peptide synthesis were fully controlled by a computer program. For the peptide synthesis on a glass chip, 20 NVOC-protected amino acids were synthesized. The coupling efficiencies of two model peptide sequences were examined on ACA/APTS and PEG/CHI/GPTS chips. PEG/CHI/GPTS chip gave higher average stepwise yields of GIYWHHY (94%) and YIYGSFK (98%) than those of ACA/APTS chip. To quantify peptide-protein binding affinity, HPQ- or HPM-containing pentapeptides were synthesized on a PEG/CHI/GPTS chip and the binding event of Cy3 labeled-streptavidin was quantified. The peptide sequence of IQHPQ showed highest binding affinity with Cy3 labeled-streptavidin. The results demonstrated that the photolithographic peptide array synthesis method efficiently quantified the binding activities of protein-peptide interactions and it can be used for additional biological assay applications.

Synthesis of pentafluorophenyl esters of nitroveratryloxycarbonyl-protected amino acids

For efficient peptide synthesis on a glass chip, 20 kinds of pentafluorophenyl (Pfp) esters of nitroveratryloxycarbonyl (NVOC)-protected amino acids were synthesized by using Pfp trifluoroacetate. Simple purification step gave moderate to high yield. The first loading time of each amino acid on glass surface was 30-60 min. The UV cleavage of the NVOC group was completed within 10 minutes. Georg Thieme Verlag Stuttgart - New York.