Minimization of apoptosis-inducing CPP-Bim peptide

Shengli Zhou; Kazunori Watanabe; Seiichiro Koide; Mizuki Kitamatsu; Takashi Ohtsuki

doi:10.1016/j.bmcl.2021.127811

Minimization of apoptosis-inducing CPP-Bim peptide

Bioorg Med Chem Lett. 2021 Mar 15:36:127811. doi: 10.1016/j.bmcl.2021.127811. Epub 2021 Jan 21.

Authors

Shengli Zhou¹, Kazunori Watanabe¹, Seiichiro Koide², Mizuki Kitamatsu², Takashi Ohtsuki³

Affiliations

¹ Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
² Department of Applied Chemistry, Kindai University, 3-4-1 Kowakae, Higashi-Osaka, Osaka 577-8502, Japan.
³ Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan. Electronic address: [email protected].

PMID: 33486053
DOI: 10.1016/j.bmcl.2021.127811

Abstract

Pro-apoptotic peptides may be promising agents for cancer therapy owing to their ability to induce apoptosis in cancer cells. TatBim, a fusion peptide of Tat cell-penetrating peptide (CPP) and the BH3 domain derived from Bim apoptosis-inducing protein, is a pro-apoptotic peptide. In this study, based on the TatBim sequence, we attempted to minimize the CPP-Bim peptide while retaining apoptosis-inducing activity. The CPP and Bim parts were systematically shortened, and the pro-apoptotic activities of the shortened peptides were examined. We obtained TatBim-N1C2 and R8Bim-N1C2 as minimized peptides with efficient apoptotic activity. These peptides may have potential applications in future biomedical studies, such as cancer therapeutics.

Keywords: Apoptosis; Bim; Cell penetrating peptide; Poly(Arg); Tat.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Apoptosis / drug effects*
Apoptosis Regulatory Proteins / chemistry
Apoptosis Regulatory Proteins / metabolism*
Cell-Penetrating Peptides / chemistry
Cell-Penetrating Peptides / pharmacology*
HeLa Cells
Humans

Substances

Apoptosis Regulatory Proteins
Cell-Penetrating Peptides