Cas no 52329-46-1 (H-Pro-Tyr-NH2·HCl)

H-Pro-Tyr-NH2·HCl is a dipeptide derivative consisting of proline (Pro) and tyrosine (Tyr) with an amide C-terminus and an HCl salt form. This compound is commonly utilized in peptide synthesis and biochemical research due to its stable structure and high purity. The presence of the tyrosine residue allows for potential modifications, such as radiolabeling or fluorescence tagging, making it valuable in studies involving receptor binding or enzyme activity. The HCl salt form enhances solubility in aqueous solutions, facilitating handling in laboratory applications. Its well-defined chemical properties ensure reproducibility in experimental settings, supporting its use in pharmaceutical and proteomics research.
H-Pro-Tyr-NH2·HCl structure
H-Pro-Tyr-NH2·HCl structure
Product Name:H-Pro-Tyr-NH2·HCl
CAS No:52329-46-1
MF:C14H19N3O3
MW:277.318963289261
CID:359892
PubChem ID:3075753
Update Time:2025-06-11

H-Pro-Tyr-NH2·HCl Chemical and Physical Properties

Names and Identifiers

    • L-Tyrosinamide, L-prolyl-
    • (2S)-N-[(2S)-1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]pyrrolidine-2-carboxamide
    • H-Pro-Tyr-NH?·HCl
    • H-PRO-TYR-NH2 · HCL
    • 52329-46-1
    • CHEMBL99658
    • prolyltyrosine amide
    • DTXSID60388952
    • H-Pro-Tyr-NH2·HCl
    • Inchi: 1S/C14H19N3O3/c15-13(19)12(8-9-3-5-10(18)6-4-9)17-14(20)11-2-1-7-16-11/h3-6,11-12,16,18H,1-2,7-8H2,(H2,15,19)(H,17,20)/t11-,12-/m0/s1
    • InChI Key: FYSOVNFPTBIWBY-RYUDHWBXSA-N
    • SMILES: O=C([C@@H]1CCCN1)N[C@H](C(N)=O)CC1C=CC(=CC=1)O

Computed Properties

  • Exact Mass: 277.14277
  • Monoisotopic Mass: 277.14264148g/mol
  • Isotope Atom Count: 0
  • Hydrogen Bond Donor Count: 4
  • Hydrogen Bond Acceptor Count: 6
  • Heavy Atom Count: 20
  • Rotatable Bond Count: 6
  • Complexity: 354
  • Covalently-Bonded Unit Count: 1
  • Defined Atom Stereocenter Count: 2
  • Undefined Atom Stereocenter Count : 0
  • Defined Bond Stereocenter Count: 0
  • Undefined Bond Stereocenter Count: 0
  • XLogP3: -0.8
  • Topological Polar Surface Area: 104?2

Experimental Properties

  • PSA: 104.45

H-Pro-Tyr-NH2·HCl Pricemore >>

Related Categories No. Product Name Cas No. Purity Specification Price update time Inquiry
TRC
H227340-250mg
H-Pro-Tyr-NH2·HCl
52329-46-1
250mg
$ 620.00 2022-06-04
TRC
H227340-500mg
H-Pro-Tyr-NH2·HCl
52329-46-1
500mg
$ 1025.00 2022-06-04
TRC
H227340-1000mg
H-Pro-Tyr-NH2·HCl
52329-46-1
1g
$ 1640.00 2022-06-04

Additional information on H-Pro-Tyr-NH2·HCl

Professional Introduction to H-Pro-Tyr-NH2·HCl (CAS No. 52329-46-1)

H-Pro-Tyr-NH2·HCl, a compound with the chemical name N-Hydroxyprolyltyrosine hydrochloride, is a synthetic peptide derivative that has garnered significant attention in the field of pharmaceutical research and biotechnology. This compound, identified by its unique CAS No. 52329-46-1, is widely recognized for its potential applications in drug development, particularly in the synthesis of bioactive peptides and as a precursor in the production of therapeutic agents.

The structure of H-Pro-Tyr-NH2·HCl consists of a proline (Pro) and tyrosine (Tyr) residue linked by an amide bond, with a hydroxyl group (-OH) attached to the proline moiety and a terminal amino group (-NH2) at the tyrosine residue. The hydrochloride salt form enhances its solubility in aqueous solutions, making it more suitable for various biochemical applications.

In recent years, there has been growing interest in the development of novel peptide-based therapeutics due to their high specificity and low toxicity. H-Pro-Tyr-NH2·HCl has emerged as a key intermediate in the synthesis of complex peptides, including those used in targeted cancer therapies and anti-inflammatory agents. Its role in peptide coupling reactions has been extensively studied, particularly in solid-phase peptide synthesis (SPPS), where it serves as a building block for constructing larger peptide chains.

One of the most compelling aspects of N-Hydroxyprolyltyrosine hydrochloride is its involvement in enzymatic reactions and post-translational modifications. The hydroxyl group on the proline residue can participate in hydrogen bonding networks, influencing the conformational stability of peptides. This property makes it particularly valuable in designing peptides with specific biological activities, such as those targeting protein-protein interactions or modulating enzyme function.

Recent research has highlighted the potential of H-Pro-Tyr-NH2·HCl in the development of peptide-based vaccines. Its ability to form stable complexes with other biomolecules has been exploited to create multivalent vaccine candidates that can elicit robust immune responses. Studies have demonstrated its efficacy in formulations designed to enhance antigen presentation and T-cell activation, paving the way for novel immunotherapeutic strategies.

The pharmaceutical industry has also explored N-Hydroxyprolyltyrosine hydrochloride as a component in drug delivery systems. Its amphiphilic nature allows it to form micelles or nanoparticles when combined with other hydrophobic and hydrophilic compounds. These nanoformulations have shown promise in improving the bioavailability and targeted delivery of therapeutic agents, particularly for drugs that require protection from enzymatic degradation or have poor solubility.

Moreover, CAS No. 52329-46-1 has been utilized in academic research to investigate the mechanisms of peptide-protein interactions. Its well-defined structure and reactivity make it an ideal candidate for computational modeling and experimental studies aimed at understanding how peptides bind to their targets. Such insights are crucial for designing next-generation therapeutics with enhanced efficacy and reduced off-target effects.

In conclusion, H-Pro-Tyr-NH2·HCl represents a versatile and valuable compound in modern pharmaceutical research. Its applications span from serving as a key intermediate in peptide synthesis to being a critical component in drug delivery systems and vaccine development. The ongoing exploration of its biological activities and structural properties continues to expand its potential uses, making it an indispensable tool for researchers striving to innovate in the field of biomedicine.

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