Inhibitors containing Unusual Amino Acids

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Inhibitors containing Unusual Amino Acids


CAS 1218-34-4
Catalog BAT-003856
Molecular Weight 246.30
Molecular Formula C13H14N2O3

Nα-Benzoyl-L-arginine amide hydrochloride

CAS 4299-03-0
Catalog BAT-003857
Molecular Weight 313.80
Molecular Formula C13H19N5O2·HCl
Nα-Benzoyl-L-arginine amide hydrochloride


CAS 20767-00-4
Catalog BAT-003858
Molecular Weight 313.30
Molecular Formula C11H11N3O8

L-Azetidine-2-carboxylic acid

CAS 2133-34-8
Catalog BAT-005580
Molecular Weight 101.10
Molecular Formula C4H7NO2
L-Azetidine-2-carboxylic acid

β-Alanine methyl ester hydrochloride

CAS 3196-73-4
Catalog BAT-007609
Molecular Weight 139.62
Molecular Formula C4H9NO2·HCl
β-Alanine methyl ester hydrochloride

Boc-L-aspartic acid β-methyl ester

CAS 59768-74-0
Catalog BAT-007635
Molecular Weight 247.25
Molecular Formula C10H17NO7
Boc-L-aspartic acid β-methyl ester


CAS 2731-73-9
Catalog BAT-007773
Molecular Weight 123.54
Molecular Formula C3H6NO2Cl

2-Aminoindane-2-carboxylic acid

CAS 27473-62-7
Catalog BAT-007785
Molecular Weight 177.20
Molecular Formula C10H11NO2
2-Aminoindane-2-carboxylic acid

2-Aminotetraline-2-carboxylic acid

CAS 6331-63-1
Catalog BAT-007786
Molecular Weight 191.22
Molecular Formula C11H13NO2
2-Aminotetraline-2-carboxylic acid


CAS 1483-07-4
Catalog BAT-007822
Molecular Weight 147.13
Molecular Formula C4H9N3O3


CAS 14091-08-8
Catalog BAT-007861
Molecular Weight 199.63
Molecular Formula C9H10ClNO2

4-Chloro-D-phenylalanine methyl ester hydrochloride

CAS 33965-47-8
Catalog BAT-007862
Molecular Weight 250.12
Molecular Formula C10H12ClNO2·HCl
4-Chloro-D-phenylalanine methyl ester hydrochloride


CAS 94-09-7
Catalog BAT-008081
Molecular Weight 165.19
Molecular Formula C9H11NO2

S 3304

CAS 203640-27-1
Catalog BAT-008640
Molecular Weight 464.6
Molecular Formula C24H20N2O4S2
S 3304

Remdesivir p-NitroPhenoxy L-Alanine Impurity

CAS 1354823-36-1
Catalog BAT-008757
Molecular Weight 450.4
Molecular Formula C21H27N2O7P
Remdesivir p-NitroPhenoxy L-Alanine Impurity

(S)-2-Amino-3-(methylamino)propanoic acid hydrochloride

CAS 16012-55-8
Catalog BAT-008963
Molecular Weight 154.59
Molecular Formula C4H11ClN2O2
(S)-2-Amino-3-(methylamino)propanoic acid hydrochloride


CAS 110117-83-4
Catalog BAT-008976
Molecular Weight 218.25
Molecular Formula C12H14N2O2


CAS 66701-25-5
Catalog BAT-015060
Molecular Weight 357.41
Molecular Formula C15H27N5O5


CAS 88321-09-9
Catalog BAT-015061
Molecular Weight 342.43
Molecular Formula C17H30N2O5


CAS 88909-96-0
Catalog BAT-015357
Molecular Weight 283.28
Molecular Formula C16H13NO4


Inhibitors containing unusual amino acids refer to the collection of all inhibitors containing unnatural amino acids in the molecular structure, such as peptide inhibitors, protease inhibitors, kinase inhibitors and so on.

The number of functional groups carried by 20 natural amino acids is limited, which can not meet the needs of protein structure and function in chemical and biological research and application. Unnatural amino acids artificially endowed with diverse functional groups are outstanding in protein modification. These unusual amino acids contain diverse functional groups such as ketone, aldehyde, azide, alkynyl, alkenyl, amide, nitro, phosphate and sulfonate, which can carry out a variety of modification reactions, such as click chemistry, photochemistry, glycosylation, fluorescence color development and so on. The modification of proteins by inhibitors containing unusual amino acids has brought new opportunities for the theoretical research and application of their structure and function.

Modification method and process

  1. Chemical synthesis
  2. Inhibitors containing unusual amino acids can be synthesized by the combination of solid-phase peptide synthesis and semi synthesis. However, the application of this technology is limited by the chemical properties of the required protective groups, connecting sites, protein folding and so on.

  3. Biosynthesis in vitro
  4. Biosynthesis in vitro can couple tRNA from connected natural amino acids and combine tRNA with unusual amino acids. Then, the cell translation system uses these aminoacylated tRNAs with unusual amino acids to synthesize inhibitors containing unusual amino acids under the corresponding blank codon or coding codon.

  5. Microinjection method
  6. In vivo, site-specific modification of proteins by microinjection technology comes from the expansion of biosynthesis methods in vitro. However, it inherits the shortcomings of the biosynthesis method in vitro, that is, the aminoacylated tRNA cannot be reused and can only be applied to the cell mouth that can be microinjected.

  7. Post translation modification
  8. Post-translational modification of protein plays a very important role in life. It makes the structure of inhibitors containing unusual amino acids more complex, the regulation more fine and the function more specific. The common post-translational modification processes include ubiquitination, phosphorylation, glycosylation, liposylation, methylation and acetylation.


  1. For bio-catalysis
  2. Inhibitors containing unusual amino acids, such as enzyme inhibitors, could play an efficient role in organic solvents after chemical modification. Meanwhile, at the same temperature, the hydrogen bond in natural protein molecules will break, resulting in structural changes and protein denaturation. Inhibitors containing unnatural amino acids enhance thermal stability.

  3. For drug development
  4. Inhibitors containing unusual amino acids has selectivity to related transporters and can block the uptake of neutral amino acids in mouse small intestine turnover model, so it can be used to treat diabetes. Inhibitors containing unusual amino acids can specifically target mitochondria, interact with mitochondrial outer membrane protein, cause mitochondrial dysfunction, and then cause mitochondrial autophagy to play an anti-tumor role.

  5. As functional probe
  6. The combination of inhibitors containing unusual amino acids and related atoms can be used to clarify the conformational changes of related proteins at ligand sites, and can also explain the complex dynamic phenomena of mammalian related proteins.

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