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Volumn 10, Issue 1, 2000, Pages 13-16

Design, synthesis and structure-activity relationship of a series of arginine aldehyde factor Xa inhibitors. Part 1: Structures based on the (D)- Arg-Gly-Arg tripeptide sequence

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE DERIVATIVE; ARGININE DERIVATIVE; BLOOD CLOTTING FACTOR 10A INHIBITOR;

EID: 0034598319     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(99)00582-X     Document Type: Article
Times cited : (28)

References (24)
  • 9
    • 0343222572 scopus 로고
    • EP 0 542 525 A2
    • Shuman, R. T. EP 0 542 525 A2. Chem. Abstr. 1993, 119, 250510.
    • (1993) Chem. Abstr. , vol.119 , pp. 250510
    • Shuman, R.T.1
  • 10
    • 0342353069 scopus 로고    scopus 로고
    • Boc Arg(Cbz)OH is also commercially available from Bachem, A-4055
    • Boc Arg(Cbz)OH is also commercially available from Bachem, A-4055.
  • 11
    • 0342353068 scopus 로고    scopus 로고
    • The tripeptide aldehydes were identified by their characteristic HPLC trace showing at least three peaks presumably reflecting the equilibrium between the free aldehyde, the hydrate, and the two diasteriomeric cyclic aminal forms. Purification is performed by RP-HPLC using a water/acetonitrile/0.1% TFA gradient. All final compounds were characterized by electrospray mass spectrometry as well as by their ability to react with DNPH
    • The tripeptide aldehydes were identified by their characteristic HPLC trace showing at least three peaks presumably reflecting the equilibrium between the free aldehyde, the hydrate, and the two diasteriomeric cyclic aminal forms. Purification is performed by RP-HPLC using a water/acetonitrile/0.1% TFA gradient. All final compounds were characterized by electrospray mass spectrometry as well as by their ability to react with DNPH.
  • 13
    • 0027990502 scopus 로고    scopus 로고
    • 50 is determined from a 4-parameter curve of the data using SOFTmax software. The prothrombinase inhibition assay was performed in a plasma free system with modifications to the method described by Sinha, U.; Hancock, T. E.; Nzerem, J. J.; Lin, P.-H; Tomlinson, J. E.; Wolf, D. L. Thrombosis Research 1994, 75, 427
    • 50 is determined from a 4-parameter curve of the data using SOFTmax software. The prothrombinase inhibition assay was performed in a plasma free system with modifications to the method described by Sinha, U.; Hancock, T. E.; Nzerem, J. J.; Lin, P.-H; Tomlinson, J. E.; Wolf, D. L. Thrombosis Research 1994, 75, 427.
  • 14
    • 0343658200 scopus 로고    scopus 로고
    • 15 it is not know what the substrate activity is with the prothrombinase complex
    • 15 it is not know what the substrate activity is with the prothrombinase complex.
  • 15
    • 0342787977 scopus 로고
    • US Patent No. 4,797,472, 110:232106
    • Gastavsson S.I., Arielly S. US Patent No. 4,797,472, 110:232106. Chem. Abstr. 110:1989;250510.
    • (1989) Chem. Abstr. , vol.110 , pp. 250510
    • Gastavsson, S.I.1    Arielly, S.2
  • 18
    • 0342787975 scopus 로고    scopus 로고
    • 4 is prepared by reacting the free amino group of the lysine sidechain of Boc-D-Lys-Gly-Arg-H with excess HBTU and DIEA. The product was confirmed by ES-MS
    • 4 is prepared by reacting the free amino group of the lysine sidechain of Boc-D-Lys-Gly-Arg-H with excess HBTU and DIEA. The product was confirmed by ES-MS.
  • 20
    • 0343222570 scopus 로고    scopus 로고
    • 50s (μM) are noted for argininals 3, 20: bovine trypsin (0.048, 0.024), t-PA (32.2, 4.4), plasmin (8.1, 1.1), aPC (56.4, 6.9), kallikrein (4.1, 0.38)
    • 50s (μM) are noted for argininals 3, 20: bovine trypsin (0.048, 0.024), t-PA (32.2, 4.4), plasmin (8.1, 1.1), aPC (56.4, 6.9), kallikrein (4.1, 0.38).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.