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Inhibition of Ras-Effector Interaction by Cyclic Peptides.


ABSTRACT: A combinatorial library of 6 × 106 cyclic peptides was synthesized in the one bead-two compound format, with each bead displaying a unique cyclic peptide on its surface and a linear peptide encoding tag in its interior. Screening of the library against K-Ras identified compounds that bound K-Ras with submicromolar affinity and disrupted its interaction with effector proteins.

SUBMITTER: Wu X 

PROVIDER: S-EPMC3621770 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature

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Inhibition of Ras-Effector Interaction by Cyclic Peptides.

Wu Xianghong X   Upadhyaya Punit P   Villalona-Calero Miguel A MA   Briesewitz Roger R   Pei Dehua D  

MedChemComm 20130201 2


A combinatorial library of 6 × 10<sup>6</sup> cyclic peptides was synthesized in the one bead-two compound format, with each bead displaying a unique cyclic peptide on its surface and a linear peptide encoding tag in its interior. Screening of the library against K-Ras identified compounds that bound K-Ras with submicromolar affinity and disrupted its interaction with effector proteins. ...[more]

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