Toxicity Data
LC50 (Rat) = 159 mg/m³/6h

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800 mg/kg For more complete non-human toxicity data on dicyclohexylcarbodiimide (6 items in total), please visit the HSDB records page.

N,n'-Dicyclohexylcarbodiimide is a white crystalline solid with a strong sweet aroma. (NTP, 1992)
1,3-Dicyclohexylcarbodiimide is a carbodiimide compound with cyclohexyl substituents on both nitrogen atoms. It can be used as a peptide coupling agent, ATP synthase inhibitor, and cross-linking agent.
A carbodiimide used as a chemical intermediate and coupling agent in peptide synthesis. (From Holly's Concise Dictionary of Chemistry, 12th Edition)
Mechanism of Action

The molecular mechanism of the neutral organic cation/H+ antitransporter in renal brush border membrane vesicles was studied using the typical organic cation N1-methylnicotinamide. The hydrophobic carbodiimide N,N'-dicyclohexylcarbodiimide (DCCD) has an IC50 of 2.6 μM at pH 7.5 and 40 nM at pH 6.0, and irreversibly inhibits the transport of organic cations. On the other hand, the hydrophilic reagents 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide and N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline do not affect the transport of organic cations. The substrate does not affect the inactivation rate of DCCD, which follows pseudo-first-order kinetics. The apparent rate constant versus DCCD concentration is linear with a slope of 0.8. The data are consistent with a simple bimolecular reaction mechanism, indicating that one DCCD molecule inactivates one carboxylic acid group in each active transport unit, and that this carboxylic acid group is crucial for transport. The hydrophobic carbodiimide dicyclohexylcarbodiimide (DCCD) has been shown to inhibit the catalytic (C) subunit of adenosine cyclic adenosine monophosphate-dependent protein kinase (EC 2.7.1.3) in a time-dependent, irreversible manner. The inactivation rate is first-order and exhibits saturation kinetics, with an apparent Ki value of 60 μM. Magnesium adenosine 5'-triphosphate (MgATP) resisted this inhibition, while neither the synthetic peptide substrate nor histones provided protection. MgATP alone provided some protection. No inhibition was observed when the catalytic subunit aggregated with the regulatory subunit to form a holoenzyme complex. The inhibition was enhanced at low pH, indicating that the carboxylic acid group is the target of DCCD interaction. Based on the protection experiments, this carboxylic acid group is likely associated with the MgATP binding site, perhaps as a metal ligand. To determine the DCCD modification site, we performed the following experiments: (1) modification with [14C]DCCD; (2) modification with DCCD in the presence of [3H]aniline; (3) modification with DCCD and [14C]glycine ethyl ester. No radioactive incorporation was detected in any of the experiments, indicating that the irreversible inhibition was caused by intramolecular crosslinking between the active carboxylic acid group and the adjacent amino group. Differential peptide mapping identified a peptide that was continuously lost due to DCCD inhibition. This peptide (residues 166-189) contained four carboxylic acid residues and one internal lysine residue.
Dicyclohexylcarbodiimide (DCCD) specifically inhibits the F1F0-H+-ATP synthase complex in E. coli by covalently modifying a protein lipid subunit embedded in the membrane. Multiple copies of the DCCD reactive protein, also known as subunit c, are present in the F1F0 complex. ...
A spontaneous mutant strain of Methanothermobacter thermautotrophicus resistant to the ATP synthase inhibitor N,N'-dicyclohexylcarbodiimide (DCCD) was isolated. DCCD typically inhibits methanogenic electron transport-driven ATP synthesis; however, this DCCD-resistant strain still exhibited methanogenic activity in the presence of 300 μmol/L DCCD. The results indicate that the total ATP synthesis of the mutant strain was higher than that of the wild-type strain regardless of the presence of DCCD. These results suggest that the ATP synthesis system of the mutant strain has been altered. Blue electrophoresis combined with MALDI-TOF/TOF mass spectrometry analysis revealed elevated concentrations of both the A(1) and A(o) subcomplexes of A(1)A(o) ATP synthase in the mutant strain. However, no alterations were found in the structural gene (atp) of A(1)A(o) ATP synthase. These results indicate that DCCD resistance is a consequence of increased expression of A(1)A(o) ATP synthase, suggesting that genes involved in regulating this enzyme expression are responsible for DCCD resistance.

C13H22N2

206.3272

206.178

538-75-0

10868

Colorless to off-white <34°C powder,>35°C liquid

1.325

122-124 ºC (6 torr)

34-35 °C(lit.)

87 ºC

0.0±0.5 mmHg at 25°C

1.567

5.54

0

2

2

15

201

0

N(=C=NC1([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C1([H])[H])C1([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C1([H])[H]

QOSSAOTZNIDXMA-UHFFFAOYSA-N

InChI=1S/C13H22N2/c1-3-7-12(8-4-1)14-11-15-13-9-5-2-6-10-13/h12-13H,1-10H2

2934.99.9001

Powder      -20°C    3 years

                     4°C     2 years

In solvent   -80°C    6 months

                  -20°C    1 month

Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)

DMSO : ~100 mg/mL (~484.66 mM)

Solubility in Formulation 1: ≥ 2.5 mg/mL (12.12 mM) (saturation unknown) in 10% DMSO + 40% PEG300 + 5% Tween80 + 45% Saline (add these co-solvents sequentially from left to right, and one by one), clear solution.
For example, if 1 mL of working solution is to be prepared, you can add 100 μL of 25.0 mg/mL clear DMSO stock solution to 400 μL PEG300 and mix evenly; then add 50 μL Tween-80 to the above solution and mix evenly; then add 450 μL normal saline to adjust the volume to 1 mL.
Preparation of saline: Dissolve 0.9 g of sodium chloride in 100 mL ddH₂ O to obtain a clear solution.

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Solubility in Formulation 2: ≥ 2.5 mg/mL (12.12 mM) (saturation unknown) in 10% DMSO + 90% (20% SBE-β-CD in Saline) (add these co-solvents sequentially from left to right, and one by one), clear solution.
For example, if 1 mL of working solution is to be prepared, you can add 100 μL of 25.0 mg/mL clear DMSO stock solution to 900 μL of 20% SBE-β-CD physiological saline solution and mix evenly.
Preparation of 20% SBE-β-CD in Saline (4°C，1 week): Dissolve 2 g SBE-β-CD in 10 mL saline to obtain a clear solution.

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Solubility in Formulation 3: ≥ 2.5 mg/mL (12.12 mM) (saturation unknown) in 10% DMSO + 90% Corn Oil (add these co-solvents sequentially from left to right, and one by one), clear solution.
For example, if 1 mL of working solution is to be prepared, you can add 100 μL of 25.0 mg/mL clear DMSO stock solution to 900 μL of corn oil and mix evenly.

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 (Please use freshly prepared in vivo formulations for optimal results.)