Design and biological testing of peptidic dimerization inhibitors of human Hsp90 that target the C-terminal domain
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- 作者：Bertan Boppa ; 1 ; Emanuele Cigliab ; 1 ; Anissa Ouald-Chaibb ; Georg Grothc ; Holger Gohlkeb ; 2 ; Gohlke@uni-duesseldorf.de" class="auth_mail" title="E-mail the corresponding author ; Joachim Josea ; 2 ; joachim.jose@uni-muenster.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：Hsp90 ; Heat shock protein 90 ; PPI ; Protein&ndash ; protein interaction ; MD ; Molecular dynamics ; CD ; Circular dichroism ; MST ; Microscale thermophoresis
- 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
- 出版年：2016
- 出版时间：June 2016
- 年：2016
- 卷：1860
- 期：6
- 页码：1043-1055
- 全文大小：3276 K
文摘
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Three peptides were designed to block the dimerization of Hsp90.
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Structural properties of these peptides were examined using MD simulations and CD spectroscopy.
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An Autodisplay based flow cytometer assay was developed to test the inhibitory effect of these peptides.
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Microscale thermophoresis was used to determine the KD of two of the peptides towards the C-terminal domain of Hsp90.
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These peptides are the first known inhibitors of Hsp90 dimerization shown to target the C-terminal domain.