From Erythropoietin to Its Peptide Derivatives: Smaller but Stronger

Author(s): Chao Zhang , Cheng Yang , Tongyu Zhu* .

Journal Name: Current Protein & Peptide Science

Volume 18 , Issue 12 , 2017

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Abstract:

Erythropoietin (EPO), recognized early as a tissue protective agent, can trigger antiinflammatory and anti-apoptotic processes to delimit injury and promote repair by binding tissueprotective receptor (TPR). However, only at a high dosage can EPO exert tissue protective effect, which may elicit severe side-effects at the meantime. Helix B surface peptide (HBSP), a 11-amnio acid sequence derived from the non-erythropoietic helix B of EPO, not only shows higher affinity to TPR but also plays a more specific and powerful role in tissue protection without erythropoietic side-effects. While it has obvious merits, the 2-min plasma half-life of HBSP restricts its application in vivo. Therefore, based on the amino acid sequence of HBSP, we originally designed and synthesized thioethercyclized helix B peptide (CHBP) for an increased resistance to proteolytic degradation as well as an improved tissue protective potency, implying a brighter prospective for translational application. In this review, we will mainly discuss the development from EPO to CHBP, the merits and limitation of CHBP and the probable mechanism mediating tissue protection.

Keywords: Erythropoietin, HBSP, CHBP, ischemia-reperfusion injury, tissue protection, derivatives.

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Article Details

VOLUME: 18
ISSUE: 12
Year: 2017
Page: [1191 - 1194]
Pages: 4
DOI: 10.2174/1389203717666160909130006
Price: $58

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