30034-25-4

Upstream product

• 63-91-2 L-phenylalanine 
• 42855-00-5 nitroveratryloxycarbonyl chloride 

Downstream Products

• 132018-86-1 N-NVOC-L-phenylalanine cyanomethyl ester 
• 58822-25-6 Leu-enkephalin 
• 132019-03-5 pdCpA<2'-O-(H-Phe)> 
• 132019-04-6 pdCpA<3'-O-(H-Phe)> 
• 132076-56-3 5'-phospho-2'-deoxycytidylyl(3'-5')-2'-O-adenosine 
• 132076-57-4 5'-phospho-2'-deoxycytidylyl(3'-5')-3'-O-adenosine 
• 1209481-02-6 C₂₅H₁₉F₅N₂O₈ 
• 63-91-2 L-phenylalanine 

Relevant academic research and scientific papers

Oligonucleotide promoted peptide bond formation using a tRNA mimicking approach

TransferRNA's role in protein translation is the prime example of an Informational Leaving Group (ILG). A simplified model produced oligophenylalanine with a modified uracil as an ILG in the presence of specific oligonucleotides. Our preliminary studies contribute to the importance of hybrid species in bridging the gap between peptides and nucleic acids.

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.

Sequentially photocleavable protecting groups in solid-phase synthesis

(Matrix presented) A sequential solid-phase peptide synthesis was developed using both photolabile linker and protecting groups. The chromatic sequential lability between a tert-butyl ketone-derived linker (sensitive to irradiation at 305 nm) and a nitroveratryloxycarbonyl (NVOC) group (sensitive at 360 nm) was exploited to prepare Leu-Enkephalin in a 55% overall yield. This new strategy allows the preparation of peptides in essentially neutral medium, by avoiding the use of common deprotection reagents such as trifluoroacetic acid or piperidine.

A general and efficient route for chemical aminoacylation of transfer RNAs

A general and expedient procedure for the synthesis of aminoaeyl tRNA has been developed. The preparation of aminoacyl dCpA in one step and in high yield by reaction of the cyanomethyl active esters of N-protected α-amino with pdCpA is detailed. The preparation and photodeprotection of aminoacyl pdCpA derivatives containing nitroveratryl (NVOC) N-protected amino acids is also studied. The utility of the above methods for preparing aminoacyl tRNA was confirmed by enzymatically ligating NVOC-phenylalanyl pdCpA to tRNA-COH followed by photolysis to provide unprotected phenylalanyl tRNA. The phenylalanyl tRNA shown to be competent in an in vitro protein biosynthesis system. These protocols greatly simplify the use of chemically misacylated tRNAs in the synthesis of proteins containing unnatural ainino acids, as well as in studies of protein biosynthesis.