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(4-Benzylbenzyl)[2(S)-[N-[2,2-dimethyl-1(S)-(N-methylcarbamoyl)propyl]carbamoyl]-4-phenylbutyl]phosphinic acid is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

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  • 202976-34-9 Structure
  • Basic information

    1. Product Name: (4-Benzylbenzyl)[2(S)-[N-[2,2-dimethyl-1(S)-(N-methylcarbamoyl)propyl]carbamoyl]-4-phenylbutyl]phosphinic acid
    2. Synonyms:
    3. CAS NO:202976-34-9
    4. Molecular Formula: C32H41N2O4P
    5. Molecular Weight: 548.66837
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 202976-34-9.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: N/A
    3. Flash Point: N/A
    4. Appearance: N/A
    5. Density: N/A
    6. Refractive Index: N/A
    7. Storage Temp.: N/A
    8. Solubility: N/A
    9. CAS DataBase Reference: (4-Benzylbenzyl)[2(S)-[N-[2,2-dimethyl-1(S)-(N-methylcarbamoyl)propyl]carbamoyl]-4-phenylbutyl]phosphinic acid(CAS DataBase Reference)
    10. NIST Chemistry Reference: (4-Benzylbenzyl)[2(S)-[N-[2,2-dimethyl-1(S)-(N-methylcarbamoyl)propyl]carbamoyl]-4-phenylbutyl]phosphinic acid(202976-34-9)
    11. EPA Substance Registry System: (4-Benzylbenzyl)[2(S)-[N-[2,2-dimethyl-1(S)-(N-methylcarbamoyl)propyl]carbamoyl]-4-phenylbutyl]phosphinic acid(202976-34-9)
  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 202976-34-9(Hazardous Substances Data)

202976-34-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 202976-34-9 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,0,2,9,7 and 6 respectively; the second part has 2 digits, 3 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 202976-34:
(8*2)+(7*0)+(6*2)+(5*9)+(4*7)+(3*6)+(2*3)+(1*4)=129
129 % 10 = 9
So 202976-34-9 is a valid CAS Registry Number.

202976-34-9Downstream Products

202976-34-9Relevant articles and documents

PHOSPHINATE BASED INHIBITORS OF MATRIX METALLOPROTEASES

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, (2008/06/13)

A compound of the formula wherein R1, R2, R3, R4, R5, R6 and Ar are as defined above, useful in the treatment of a condition selected from the group consisting of arthritis, cancer, synergy with cytotoxic anticancer agents, tissue ulceration, macular dege

Phosphinate based inhibitors of matrix metalloproteases

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, (2008/06/13)

A compound of the formula wherein R1, R2, R3, R4, R5, R6 and Ar are as defined above, useful in the treatment of a condition selected from the group consisting of arthritis, cancer, synergy with cytotoxic anticancer agents, tissue ulceration, macular degeneration, restenosis, periodontal disease, epidermolysis bullosa, scleritis, in combination with standard NSAID'S and analgesics and other diseases characterized by matrix metalloproteinase activity, AIDS, sepsis, septic shock and other diseases involving the production of TNF. In addition, the compounds of the present invention may be used in combination therapy with standard non-steroidal anti-inflammatory drugs (NSAID'S) and analgesics, and in combination with cytotoxic drugs such as adriamycin, daunomycin, cis-platinim, etoposide, taxol, taxotere and other alkaloids, such as vincristine, in the treatment of cancer.

Inhibition of MMP-1 and MMP-13 with phosphinic acids that exploit binding in the S2 pocket

Reiter, Lawrence A.,Rizzi, James P.,Pandit, Jayvardan,Lasut, Michael J.,McGahee, Shunda M.,Parikh, Vinod D.,Blake, James F.,Danley, Dennis E.,Laird, Ellen R.,Lopez-Anaya, Arturo,Lopresti-Morrow, Lori L.,Mansour, Mahmoud N.,Martinelli, Gary J.,Mitchell, Peter G.,Owens, Brian S.,Pauly, Thomas A.,Reeves, Lisa M.,Schulte, Gayle K.,Yocum, Sue A.

, p. 127 - 132 (2007/10/03)

Through the use of empirical and computational methods, phosphinate- based inhibitors of MMP-1 and MMP-13 that bind into the S2 pocket of these enzymes were designed. The synthesis and testing of 2 suggested that binding was occuring as hypothesized. Structure determination of a co-crystal of 2 bound to the catalytic domain of MMP-1 confirmed the binding mode. Substituents binding into S2, S1', S2' and S3', were optimized yielding compounds with low double-digit nM IC50's against these enzymes.

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