期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 11, 期 15, 页码 2001-2006出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0960-894X(01)00354-7
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Two doxorubicin albumin conjugates (A-DP1 and A-DP2), which differ in their substrate specificity fur the matrix metalloproteinases MMP2 and MMP9. were prepared by binding maleimide doxorubicin peptide derivatives to the cysteine-34 position of human serum albumin. The incorporated octapeptide, Gly-Pro-Gln-Arg-Ile-Ala-Giy-Gln, in A-DP2 is not cleaved by activated MMP2 and MMP9 in contrast to Gly-Pro-Leu-Gly-Ile-Ala-Gly-Gln incorporated in A-DP1 that is cleaved efficiently by activated MMP2 and MMP9 liberating a doxorubicin tetrapeptide. A-DP1 showed antiproliferative activity in a murine renal cell carcinoma line in the low micromolar range (IC50 value approximate to0.2 muM). (C) 2001 Elsevier Science Ltd. All rights reserved.
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