32797-61-8

Usage

Uses

Used in Biochemical Research:
4-Aminomethyl benzamidine dihydrochloride is used as a research compound for its ability to mimic damnacanthal and inhibit the activity of kinases and proteases. This makes it a valuable tool in studying the mechanisms of these enzymes and their roles in various biological processes.
Used in Pharmaceutical Development:
In the pharmaceutical industry, 4-Aminomethyl benzamidine dihydrochloride is used as a starting material or intermediate in the synthesis of potential drug candidates. Its properties as an enzyme inhibitor can be leveraged to develop new therapeutic agents targeting specific kinases or proteases, which are often implicated in various diseases.
Used in Chemical Synthesis:
4-Aminomethyl benzamidine dihydrochloride is employed as a reagent in the synthesis of other chemical compounds. Its unique structure and reactivity make it a useful building block in the creation of more complex molecules, which can be applied in various fields, including materials science and specialty chemicals.

InChI:InChI=1/C8H11N3.2ClH/c9-5-6-1-3-7(4-2-6)8(10)11;;/h1-4H,5,9H2,(H3,10,11);2*1H

Upstream product

• 366023-02-1 (4-carbamimidoyl-benzyl)-carbamic acid benzyl ester 
• 328552-93-8 4-(aminomethyl)-N-hydroxybenzene-1-carboximidamide 
• 10406-25-4 4-aminobenzyl cyanide 
• 66389-80-8 tert-butyl N-[(4-cyanophenyl)methyl]carbamate 
• 162696-15-3 N-Boc-4-aminomethyl benzamidine 
• 63914-51-2 [(4-cyanophenyl)methyl]-carbamic acid phenylmethyl ester 
• 17201-43-3 4-cyanobenzyl bromide 
• 84466-87-5 4-(azidomethyl)benzonitrile 

Downstream Products

• 1456890-24-6 N-(4-carbamimidoylbenzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide 
• 1449371-73-6 C₁₄H₁₂N₆O₃ 
• 1449371-69-0 C₂₁H₂₀N₆O₃S 
• 1449371-67-8 C₁₆H₁₈N₆O₃S 
• 1449371-68-9 C₂₇H₂₅N₁₁O₄S 
• 1449371-74-7 C₂₀H₂₂N₄O₂S 

Relevant academic research and scientific papers

Protein-Templated Formation of an Inhibitor of the Blood Coagulation Factor Xa through a Background-Free Amidation Reaction

Protein-templated reactions enable the target-guided formation of protein ligands from reactive fragments, ideally with no background reaction. Herein, we investigate the templated formation of amides. A nucleophilic fragment that binds to the coagulation factor Xa was incubated with the protein and thirteen differentially activated dipeptides. The protein induced a non-catalytic templated reaction for the phenyl and trifluoroethyl esters; the latter was shown to be a completely background-free reaction. Starting from two fragments with millimolar affinity, a 29 nm superadditive inhibitor of factor Xa was obtained. The fragment ligation reaction was detected with high sensitivity by an enzyme activity assay and by mass spectrometry. The reaction progress and autoinhibition of the templated reaction by the formed ligation product were determined, and the structure of the protein–inhibitor complex was elucidated.

Design, synthesis, and evaluation of oxyanion-hole selective inhibitor substituents for the S1 subsite of factor Xa

Placement of an anionic group within the oxyanion hole region of the Factor Xa catalytic site substantially enhances activity, with small flexible groups favored over bulkier ones.

Thrombin inhibitors having a lactam at P3

The present invention provides compounds having a lactam ring at P3 and at P1 have a six-membered heterocyclic ring having two ring nitrogen ring atoms and the remainder of the ring atoms carbon atoms. These compounds have biological activity as active and potent inhibitors of thrombin. Their pharmaceutically acceptable salts, pharmaceutical compositions thereof and methods of using these compounds and pharmaceutical compositions comprising these compounds as therapeutic agents for treatment of disease states in mammals which are characterized by abnormal thrombosis are also described.

Non-covalent inhibitors of urokinase and blood vessel formation

Novel compounds having activity as non-covalent inhibitors of urokinase and having activity in reducing or inhibiting blood vessel formation are provided. These compounds have P1 a group having an amidino or guanidino moiety or derivative thereof. These compounds are useful in vitro for monitoring plasminogen activator levels and in vivo in treatment of conditions which are ameliorated by inhibition of or decreased activity of urokinase and in treating pathologic conditions wherein blood vessel formation is related to a pathologic condition.

Non-covalent inhibitors of urokinase and blood vessel formation

Novel compounds having activity as non-covalent inhibitors of urokinase and having activity in reducing or inhibiting blood vessel formation are provided. These compounds have Pi a group having an amidino or guanidino moiety or derivative thereof. These compounds are useful in vitro for monitoring plasminogen activator levels and in vivo in treatment of conditions which are ameliorated by inhibition of or decreased activity of urokinase and in treating pathologic conditions wherein blood vessel formation is related to a pathologic condition.

Novel, potent non-covalent thrombin inhibitors incorporating P3-lactam scaffolds

Evolution of P1-argininal inhibitor prototypes led to a series of non-covalent P3-7-membered lactam inhibitors 1a-w, featuring novel peptidomimetic units that probe each of the S1, S2, and S3 specificity pockets of thrombin. Rigid P1-arginine surrogates possessing a wide range of basicity (calcd pKa's～neutral-14) were surveyed. The design, synthesis, and biological activity of these targets are presented.

Dibasic inhibitors of human mast cell tryptase. Part 3: Identification of a series of potent and selective inhibitors containing the benzamidine functionality

A survey of charged groups and linkers for a series of symmetrical and unsymmetrical dibasic inhibitors is described, leading to several classes of potent and selective inhibitors. In particular, the benzamidine functionality was identified as the most potent charged group investigated.