Citation: Wu Zhi-Meng, Liu Shao-Zhong, Cheng Xiao-Zhong, Zhao Xin-Rui, Hong Hao-Fei. High yield synthesis of cyclic analogues of antibacterial peptides P-113 by Sortase A-mediated ligation and their conformation studies[J]. Chinese Chemical Letters, ;2017, 28(3): 553-557. doi: 10.1016/j.cclet.2016.11.001 shu

High yield synthesis of cyclic analogues of antibacterial peptides P-113 by Sortase A-mediated ligation and their conformation studies

The Key Laboratory of Carbohydrate Chemistry & Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China

Corresponding author: Wu Zhi-Meng, zwu@jiangnan.edu.cn
Received Date: 29 July 2016
Revised Date: 30 September 2016
Accepted Date: 9 October 2016
Available Online: 10 March 2016

Figures(5)

P-113 is a fragment of natural occurring peptide Histatin 5 found in human saliva. This peptide exhibited broad spectrum of antibacterial and antifungal biological activities. In this study, bifunctional P-113 peptides 2-5 were designed as Sortase A substrates and synthesized by solid support peptide synthesis, where the N-terminus were equipped with glycine and its analogues, and C-terminus were extended with LPETGGS, respectively. Under Sortase A catalyzed condition, head to tail cyclization products 7-10 were afforded in yields from 76% to 93%. The conformation insights of linear peptides 2-5 and cyclic analogues 7-10 in aqueous buffers and in trifluroethanol (TFE) analyzed by circular dichroism (CD) suggested that α-helix structures were produced progressively in hydrophobic environment independent of the cyclization, which displayed the similar behavior as parent peptide P-113.
- Antibacterial peptide,
- P-113,
- Cyclization,
- Sortase A-mediated ligation,
- Conformation,
- Circular dichroism
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