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Issue 89, 2017
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Bcl-XL-binding helical peptides possessing D-Ala residues at their C-termini with the advantage of long-lasting intracellular stabilities

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Abstract

We attached D-Ala residues to cross-linked helical peptides based on the pro-apoptotic protein Bad at their C-termini. The D-Ala attachment had little influence on the secondary structures and binding abilities against Bcl-XL. The D-Ala attached helical peptides were much more stable in cells than original ones and efficiently induced apoptosis of the cells.

Graphical abstract: Bcl-XL-binding helical peptides possessing d-Ala residues at their C-termini with the advantage of long-lasting intracellular stabilities

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Publication details

The article was received on 04 Sep 2017, accepted on 14 Oct 2017 and first published on 16 Oct 2017


Article type: Communication
DOI: 10.1039/C7CC06904A
Citation: Chem. Commun., 2017,53, 12104-12107
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    Bcl-XL-binding helical peptides possessing D-Ala residues at their C-termini with the advantage of long-lasting intracellular stabilities

    K. Nogami, H. Tokumaru, G. Isokawa, T. Oyoshi, K. Fujimoto and M. Inouye, Chem. Commun., 2017, 53, 12104
    DOI: 10.1039/C7CC06904A

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