Membrane permeable cyclic peptidyl inhibitors against human Peptidylprolyl Isomerase Pin1.
Membrane permeable cyclic peptidyl inhibitors against human Peptidylprolyl Isomerase Pin1.
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DOI:
10.1021/jm901778v
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发表时间:
2010-03-25
影响因子:
7.3
通讯作者:
Pei D
中科院分区:
文献类型:
--
作者:
Liu T;Liu Y;Kao HY;Pei D
Peptidyl-prolyl isomerase Pin1 regulates the function and/or stability of phosphoproteins by altering the conformation of specific pSer/pThr-Pro peptide bonds. In this work, a cyclic peptide library was synthesized and screened against the catalytic domain of human Pin1. The selected inhibitors contained a consensus motif of D-pThr-Pip-Nal (where Pip is L-piperidine-2-carboxylic acid and Nal is L-2-naphthylalanine). Representative compounds were tested for binding to Pin1 by isothermal titration calorimetry and inhibition of Pin1 activity and the most potent inhibitors had KD (and KI) values in the low nanomolar range. Treatment of breast cancer cells with the inhibitors, which were rendered membrane permeable by attachment of an octaarginine sequence, inhibited cell proliferation and increased the protein levels of two previously established Pin1 substrates, PML and SMRT. Finally, a second generation of cell permeable Pin1 inhibitors was designed by replacing the noncritical residues within the cyclic peptide ring with arginine residues and shown to have anti-proliferative activity against the cancer cells.
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影响因子:
2.9
作者:
KOFRON, JL;KUZMIC, P;RICH, DH
通讯作者:
RICH, DH
影响因子:
2.9
作者:
Hennig, L;Christner, C;Fischer, G
通讯作者:
Fischer, G
影响因子:
21.3
作者:
Ryo, A;Nakamura, M;Lu, KP
通讯作者:
Lu, KP
影响因子:
16
作者:
Stukenberg, PT;Kirschner, MW
通讯作者:
Kirschner, MW
DOI:
10.1016/j.bbrc.2009.04.144
发表时间:
2009-07-03
影响因子:
3.1
作者:
Tatara, Yota;Lin, Yi-Chin;Uchida, Takafumi
通讯作者:
Uchida, Takafumi