Amino Acids, Nucleosides and Nucleotides

Amino Acids

We offer Fmoc-protected unnatural amino acids for the synthesis of peptides for biological research and pharmaceutical development. By introducing conformational constraints, the peptides may have one or several of the following features: 1. enhancement of peptide backbone helicity for better target binding; 2. tunable hydrophobicity for desired cellular permeability and cytotoxicity; and 3. enhancement of peptide stability against proteolytic breakdown.

Nucleosides and Nucleoside Phosphoramidites

We offer nucleosides with modifications in both the nucleic acid base and the sugar component of the molecules. Nucleoside phosphoramidites are extremely useful chemical building blocks for the chemical synthesis of RNA-targeting drugs such as antisense oligonucleotides, aptamers, and siRNAs which have exhibited promises for treating diseases including muscular dystrophy, neuropathies, and macular degeneration.

Nucleotides

dNTP, NTP, and modified nucleotides have exhibited a wide range of applications in PCR, RT-PCR, cRNA synthesis, RCA, MDA, DNA labeling, and sequencing. dNTPs are chemical building blocks in the commercial manufacture of mRNA vaccines using in vitro transcription method.

Inquire about our bulk quantities for the manufacture of oligonucleotide drug ingredients and large-scale production of mRNAs.

  • Amino Acids for Stapled Peptides
  • 2-Methylated Amino Acids
  • Peptide Labeling
  • Other Unnatural Amino Acids
  • Nucleosides
  • HNA Precursors
  • Morpholino Nucleosides
  • Nucleoside Phosphoramidites and Nucleotides
  • Amino Acids for Stapled Peptides

    Structure Details
    Product Name: (2S)-4-Azido-2-[[(9H-Fluoren-9-ylmethoxy)carbonyl]amino]-butanoic acid
    Order number: 204413
    CAS: 942518-20-9
    Purity: >=95%
    Appearance: solid
    MF: C19H18N4O4
    MW: 366.377
    MP: n.a. oC

    Description:
    The azido side chain of this product can be tied (stapled) with another adjacent alkenyl side chain pre-existed on the peptide backbone via a click chemistry
    Product Name: N6-Diazo-N2-[(9H-fluoren-9-ylmethoxy)carbonyl]-2-methyl-L-lysine
    Order number: 204415
    CAS: 1050501-64-8
    Purity: >=95%
    Appearance: solid
    MF: C22H24N4O4
    MW: 408.458
    MP: n.a. oC

    Description:
    The azido side chain of this product can be tied (stapled) with another adjacent alkenyl side chain pre-existed on the peptide backbone via a click chemistry
    Product Name: (2R)-2-[[(9H-Fluoren-9-ylmethoxy)carbonyl]amino]-2-methyl-7-azidoheptanoic acid
    Order number: 204416
    CAS: 1191429-12-5
    Purity: >=95%
    Appearance: solid
    MF: C23H26N4O4
    MW: 422.485
    MP: n.a. oC

    Description:
    The azido side chain of this product can be tied (stapled) with another adjacent alkenyl side chain pre-existed on the peptide backbone via a click chemistry
    Product Name: (2R)-2-[[(9H-Fluoren-9-ylmethoxy)carbonyl]amino]-2-methyl-8-azidooctanoic acid
    Order number: 204417
    CAS: 1191429-14-7
    Purity: >=95%
    Appearance: solid
    MF: C24H28N4O4
    MW: 436.512
    MP: n.a. oC

    Description:
    The azido side chain of this product can be tied (stapled) with another adjacent alkenyl side chain pre-existed on the peptide backbone via a click chemistry
    Product Name: (2R)-2-[[(9H-Fluoren-9-ylmethoxy)carbonyl]amino]-2-methyl-4-pentynoic acid
    Order number: 204418
    CAS: 1198791-65-9
    Purity: >=95%
    Appearance: solid
    MF: C21H19NO4
    MW: 349.386
    MP: n.a. oC

    Description:
    The alkynyl side chain of this product can be tied (stapled) with another adjacent alkenyl side chain pre-existed on the peptide backbone via a click chemistry
    Product Name: (R)-N-Fmoc-2-(3'-butenyl)alanine
    Order number: 204433
    CAS: 1311933-82-0
    Purity: >=95%
    Appearance: solid
    MF: C22H23NO4
    MW: 365.429
    MP: n.a. oC

    Description:
    This alpha-methylated amino acid is used to make the peptide bond more stable against enzymatic hydrolysis. Helicity can be locked via Grubbs' methathesis reaction.