Page last updated: 2024-12-07

(3-(n-hydroxy)carboxamido-2-benzylpropanoyl)glycine

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Related Drugs Related Conditions Protein Interactions Research Growth

The chemical name (3-(n-hydroxy)carboxamido-2-benzylpropanoyl)glycine is a bit unwieldy and doesn't readily reveal its structure or function. Let's break it down and see if we can understand its significance:

**Understanding the Structure:**

* **(3-(n-hydroxy)carboxamido-2-benzylpropanoyl)**: This part describes a specific organic molecule with a few key features:
* **Benzyl:** This refers to a phenyl group (a six-membered ring of carbon atoms) attached to a CH2 group.
* **Propanoyl:** This indicates a three-carbon chain with a carbonyl group (C=O) at one end.
* **Carboxamido:** This means the propanoyl group is linked to a nitrogen atom (amide) and also has a hydroxyl group (-OH) attached to the nitrogen.
* **Glycine:** This is the simplest amino acid, with a single hydrogen atom as its side chain.

**Putting it Together:**

This compound is likely a **modified peptide**. It consists of a glycine amino acid linked to a modified propanoyl group. The modified propanoyl group carries a benzyl group and a hydroxyl group attached to the nitrogen.

**Importance in Research:**

Without more context, it's difficult to definitively state the importance of this specific compound in research. However, based on its structure, we can make some educated guesses:

* **Peptidomimetics:** Modified peptides like this are often used as **peptidomimetics** in drug discovery. Peptidomimetics are molecules designed to mimic the structure and function of natural peptides, but with improved properties like stability, bioavailability, or selectivity.
* **Biological Activity:** The presence of the benzyl group and the hydroxyl group suggests that this compound could interact with biological targets like proteins or enzymes. It might have potential applications in areas such as:
* **Pharmacology:** Targeting specific receptors or pathways related to disease processes.
* **Materials Science:** Developing materials with novel properties, potentially through self-assembly or interaction with biological systems.

**To Learn More:**

To understand the specific importance of this compound, you would need to know its context:

* **What research area is it related to?** (e.g., cancer, neurobiology, etc.)
* **What specific biological activity is it known or suspected to have?**
* **What is its purpose in the research study?** (e.g., drug candidate, probe molecule, etc.)

**Finding More Information:**

You could try searching for this compound online using its full chemical name or a more concise description (e.g., benzyl-modified propanoyl glycine). You can also search scientific databases like PubMed or Google Scholar for publications that might mention it.

Cross-References

ID SourceID
PubMed CID124786
CHEMBL ID16779
SCHEMBL ID7325845
MeSH IDM0132237

Synonyms (9)

Synonym
hcbp-gly
CHEMBL16779 ,
(2-benzyl-3-hydroxycarbamoyl-propionylamino)-acetic acid
(r,s)(2-benzyl-3-hydroxycarbamoyl-propionylamino)-acetic acid
bdbm50002022
(3-(n-hydroxy)carboxamido-2-benzylpropanoyl)glycine
SCHEMBL7325845
DTXSID80919328
n-[2-benzyl-1,4-dihydroxy-4-(hydroxyimino)butylidene]glycine
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (4)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
NeprilysinRattus norvegicus (Norway rat)IC50 (µMol)0.00140.00100.17022.3000AID67348
NeprilysinOryctolagus cuniculus (rabbit)IC50 (µMol)0.00140.00040.66118.2000AID147214; AID147516
NeprilysinHomo sapiens (human)IC50 (µMol)0.00140.00020.54226.7000AID147393
Aminopeptidase NSus scrofa (pig)IC50 (µMol)0.00200.00053.53548.9000AID35686
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (24)

Processvia Protein(s)Taxonomy
kidney developmentNeprilysinHomo sapiens (human)
placenta developmentNeprilysinHomo sapiens (human)
proteolysisNeprilysinHomo sapiens (human)
peptide metabolic processNeprilysinHomo sapiens (human)
learning or memoryNeprilysinHomo sapiens (human)
substance P catabolic processNeprilysinHomo sapiens (human)
bradykinin catabolic processNeprilysinHomo sapiens (human)
sensory perception of painNeprilysinHomo sapiens (human)
protein catabolic processNeprilysinHomo sapiens (human)
lung developmentNeprilysinHomo sapiens (human)
hormone catabolic processNeprilysinHomo sapiens (human)
response to estrogenNeprilysinHomo sapiens (human)
creatinine metabolic processNeprilysinHomo sapiens (human)
amyloid-beta metabolic processNeprilysinHomo sapiens (human)
positive regulation of neurogenesisNeprilysinHomo sapiens (human)
neuropeptide processingNeprilysinHomo sapiens (human)
cellular response to cytokine stimulusNeprilysinHomo sapiens (human)
cellular response to UV-ANeprilysinHomo sapiens (human)
cellular response to UV-BNeprilysinHomo sapiens (human)
replicative senescenceNeprilysinHomo sapiens (human)
amyloid-beta clearanceNeprilysinHomo sapiens (human)
amyloid-beta clearance by cellular catabolic processNeprilysinHomo sapiens (human)
positive regulation of long-term synaptic potentiationNeprilysinHomo sapiens (human)
protein processingNeprilysinHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (10)

Processvia Protein(s)Taxonomy
phosphatidylserine bindingNeprilysinHomo sapiens (human)
endopeptidase activityNeprilysinHomo sapiens (human)
metalloendopeptidase activityNeprilysinHomo sapiens (human)
protein bindingNeprilysinHomo sapiens (human)
exopeptidase activityNeprilysinHomo sapiens (human)
zinc ion bindingNeprilysinHomo sapiens (human)
peptide bindingNeprilysinHomo sapiens (human)
protein homodimerization activityNeprilysinHomo sapiens (human)
oligopeptidase activityNeprilysinHomo sapiens (human)
cardiolipin bindingNeprilysinHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (19)

Processvia Protein(s)Taxonomy
cytoplasmNeprilysinHomo sapiens (human)
early endosomeNeprilysinHomo sapiens (human)
trans-Golgi networkNeprilysinHomo sapiens (human)
plasma membraneNeprilysinHomo sapiens (human)
brush borderNeprilysinHomo sapiens (human)
focal adhesionNeprilysinHomo sapiens (human)
synaptic vesicleNeprilysinHomo sapiens (human)
cell surfaceNeprilysinHomo sapiens (human)
membraneNeprilysinHomo sapiens (human)
axonNeprilysinHomo sapiens (human)
dendriteNeprilysinHomo sapiens (human)
secretory granule membraneNeprilysinHomo sapiens (human)
cytoplasmic vesicleNeprilysinHomo sapiens (human)
neuronal cell bodyNeprilysinHomo sapiens (human)
neuron projection terminusNeprilysinHomo sapiens (human)
membrane raftNeprilysinHomo sapiens (human)
synapseNeprilysinHomo sapiens (human)
extracellular exosomeNeprilysinHomo sapiens (human)
presynapseNeprilysinHomo sapiens (human)
plasma membraneNeprilysinHomo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (10)

Assay IDTitleYearJournalArticle
AID147393Inhibitory potency against neutral endopeptidase1992Journal of medicinal chemistry, Apr-03, Volume: 35, Issue:7
Potent and systemically active aminopeptidase N inhibitors designed from active-site investigation.
AID35688Inhibition of dipeptidyl amino peptidase activity in rat brain with 10 nM [3H]Leu-enkephalin as substrate1989Journal of medicinal chemistry, Jul, Volume: 32, Issue:7
New kelatorphan-related inhibitors of enkephalin metabolism: improved antinociceptive properties.
AID56053Inhibition of [3H]Leu-enkephalin binding to Dipeptidyl aminopeptidase (DAP)1988Journal of medicinal chemistry, Sep, Volume: 31, Issue:9
Retro-inverso concept applied to the complete inhibitors of enkephalin-degrading enzymes.
AID67348In vitro inhibition of enkephalinase purified from rat kidney.1985Journal of medicinal chemistry, Sep, Volume: 28, Issue:9
New bidentates as full inhibitors of enkephalin-degrading enzymes: synthesis and analgesic properties.
AID38366Inhibition of Aminopeptidase N activity in pig kidney with 10 nM [3H]Leu-enkephalin as substrate1989Journal of medicinal chemistry, Jul, Volume: 32, Issue:7
New kelatorphan-related inhibitors of enkephalin metabolism: improved antinociceptive properties.
AID35684Inhibition of [3H]Leu-enkephalin binding to aminopeptidase1988Journal of medicinal chemistry, Sep, Volume: 31, Issue:9
Retro-inverso concept applied to the complete inhibitors of enkephalin-degrading enzymes.
AID35686Inhibitory activity against rabbit kidney aminopeptidase using 10 nM of [3H]Leu-enkephalin as substrate1985Journal of medicinal chemistry, Sep, Volume: 28, Issue:9
New bidentates as full inhibitors of enkephalin-degrading enzymes: synthesis and analgesic properties.
AID147516Inhibition of [3H]Ala2-Leu-enkephalin binding to Neutral endopeptidase (NEP)1988Journal of medicinal chemistry, Sep, Volume: 31, Issue:9
Retro-inverso concept applied to the complete inhibitors of enkephalin-degrading enzymes.
AID147214Inhibition of neutral endopeptidase activity in rabbit kidney with 20 nM [3H]D-Ala2-Leu-enkephalin as substrate1989Journal of medicinal chemistry, Jul, Volume: 32, Issue:7
New kelatorphan-related inhibitors of enkephalin metabolism: improved antinociceptive properties.
AID56051Inhibitory activity against rat brain Dipeptidyl aminopeptidase using 10 nM of [3H]Leu-enkephalin as substrate1985Journal of medicinal chemistry, Sep, Volume: 28, Issue:9
New bidentates as full inhibitors of enkephalin-degrading enzymes: synthesis and analgesic properties.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (5)

TimeframeStudies, This Drug (%)All Drugs %
pre-19904 (80.00)18.7374
1990's1 (20.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other5 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]