A synthetic peptide derived from NK-lysin with activity against mycobacterium tuberculosis and its structure-function relationship

Gu Hao; Dai Rongji; Qiu Kui; Teng Zhongqiu; Wang Heyao

doi:10.1007/s10989-011-9268-6

A synthetic peptide derived from NK-lysin with activity against mycobacterium tuberculosis and its structure-function relationship

Gu Hao
, Dai Rongji
, Qiu Kui
, Teng Zhongqiu
, Wang Heyao^*

^*Corresponding author for this work

School of Life Science

Beijing Institute of Technology
Capital Medical University

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

As appearance of drug resistant and multidrug resistant strains of Mycobacterium tuberculosis, antibiotics were no longer the only way to inhibit M. tuberculosis. It was shown that the porcine peptide NK-lysin is active against various microbes by interacting with microbial membranes. The NK-lysin-derived peptide has been demonstrated to possess stronger effect. Under this motivation, we synthesized a short peptide (N22) derived from an active fragment of NK-lysin-an important antimycobaterial domain involving the loop and the α-helical structure. Furthermore, we studied its stability and biological activity in vitro. The results showed that it inhibited the growth of M. tuberculosis H37Rv and had a low toxicity to human erythrocyte.

Original language	English
Pages (from-to)	301-306
Number of pages	6
Journal	International Journal of Peptide Research and Therapeutics
Volume	17
Issue number	4
DOIs	https://doi.org/10.1007/s10989-011-9268-6
Publication status	Published - Dec 2011

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Active fragments
Antimycobacterial activity
Mycobacterium tuberculosis
NK-lysin

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10.1007/s10989-011-9268-6

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abstract = "As appearance of drug resistant and multidrug resistant strains of Mycobacterium tuberculosis, antibiotics were no longer the only way to inhibit M. tuberculosis. It was shown that the porcine peptide NK-lysin is active against various microbes by interacting with microbial membranes. The NK-lysin-derived peptide has been demonstrated to possess stronger effect. Under this motivation, we synthesized a short peptide (N22) derived from an active fragment of NK-lysin-an important antimycobaterial domain involving the loop and the α-helical structure. Furthermore, we studied its stability and biological activity in vitro. The results showed that it inhibited the growth of M. tuberculosis H37Rv and had a low toxicity to human erythrocyte.",

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T1 - A synthetic peptide derived from NK-lysin with activity against mycobacterium tuberculosis and its structure-function relationship

AU - Hao, Gu

AU - Rongji, Dai

AU - Kui, Qiu

AU - Zhongqiu, Teng

AU - Heyao, Wang

PY - 2011/12

Y1 - 2011/12

N2 - As appearance of drug resistant and multidrug resistant strains of Mycobacterium tuberculosis, antibiotics were no longer the only way to inhibit M. tuberculosis. It was shown that the porcine peptide NK-lysin is active against various microbes by interacting with microbial membranes. The NK-lysin-derived peptide has been demonstrated to possess stronger effect. Under this motivation, we synthesized a short peptide (N22) derived from an active fragment of NK-lysin-an important antimycobaterial domain involving the loop and the α-helical structure. Furthermore, we studied its stability and biological activity in vitro. The results showed that it inhibited the growth of M. tuberculosis H37Rv and had a low toxicity to human erythrocyte.

AB - As appearance of drug resistant and multidrug resistant strains of Mycobacterium tuberculosis, antibiotics were no longer the only way to inhibit M. tuberculosis. It was shown that the porcine peptide NK-lysin is active against various microbes by interacting with microbial membranes. The NK-lysin-derived peptide has been demonstrated to possess stronger effect. Under this motivation, we synthesized a short peptide (N22) derived from an active fragment of NK-lysin-an important antimycobaterial domain involving the loop and the α-helical structure. Furthermore, we studied its stability and biological activity in vitro. The results showed that it inhibited the growth of M. tuberculosis H37Rv and had a low toxicity to human erythrocyte.

KW - Active fragments

KW - Antimycobacterial activity

KW - Mycobacterium tuberculosis

KW - NK-lysin

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DO - 10.1007/s10989-011-9268-6

M3 - Article

AN - SCOPUS:81355161431

SN - 1573-3149

VL - 17

SP - 301

EP - 306

JO - International Journal of Peptide Research and Therapeutics

JF - International Journal of Peptide Research and Therapeutics

IS - 4

ER -

A synthetic peptide derived from NK-lysin with activity against mycobacterium tuberculosis and its structure-function relationship

Abstract

UN SDGs

Keywords

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