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Purchase N-Acetyl-L-hydroxyproline丨CAS 33996-33-7
N-Acetyl-L-Hydroxyproline is an N-acetylated derivative of L-hydroxyproline, a non-proteinogenic amino acid associated with collagen structure and connective tissue biology. Its cyclic amino acid framework, hydroxyl group, and acetyl functionality make it relevant to amino acid chemistry, biochemical research, and the development of specialized organic compounds. This compound may serve as a research material for investigating modified hydroxyproline derivatives and related molecular structures.
Chemical Identifiers
| InChI | InChI=1S/C7H11NO4/c1-4(9)8-3-5(10)2-6(8)7(11)12/h5-6,10H,2-3H2,1H3,(H,11,12)/t5-,6+/m1/s1 |
| InChI Key | BAPRUDZDYCKSOQ-RITPCOANSA-N |
| Smiles | CC(=O)N1C[C@@H](C[C@H]1C(=O)O)O |
| EC No. | 251-780-6 |
| MDL No. | MFCD00037339 |
| PubChem CID | 65784 |
Applications
Pharmaceutical Research and Drug Discovery
Modified amino acids are used in medicinal chemistry to investigate molecular conformation, functional-group effects, and the properties of specialized compounds. N-Acetyl-L-Hydroxyproline may serve as a research intermediate in the synthesis or evaluation of related molecules. Any potential pharmaceutical application requires appropriate experimental validation and assessment of the specific target compound.
Biochemical and Amino Acid Research
Hydroxyproline derivatives are of interest in biochemical research because of their relationship to collagen and other biological processes. N-Acetyl-L-Hydroxyproline may support studies involving chemically modified amino acids, structure–property relationships, and the behavior of hydroxyproline-based compounds in suitable experimental systems.
Organic Synthesis and Chemical Research
Collagen and Connective Tissue Research
Hydroxyproline is an important component of collagen, making hydroxyproline-related compounds relevant to research on connective tissue structure and protein chemistry. N-Acetyl-L-Hydroxyproline may be used in exploratory research involving hydroxyproline derivatives and related biochemical structures. Its suitability for direct collagen-related studies depends on the specific experimental design and should not be assumed from its structural relationship alone.
