Design, recombinant fusion expression and biological evaluation of vasoactive intestinal peptide analogue as novel antimicrobial agent

Chunlan Xu; Yu Guo; Xiangjin Qiao; Xiaoya Shang; Weining Niu; Mingliang Jin

doi:10.3390/molecules22111963

Design, recombinant fusion expression and biological evaluation of vasoactive intestinal peptide analogue as novel antimicrobial agent

Chunlan Xu, Yu Guo, Xiangjin Qiao, Xiaoya Shang, Weining Niu, Mingliang Jin

School of life sciences

Northwestern Polytechnical University Xian

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

12 Scopus citations

Abstract

Antimicrobial peptides represent an emerging category of therapeutic agents with remarkable structural and functional diversity. Modified vasoactive intestinal peptide (VIP) (VIP analogue 8 with amino acid sequence “FTANYTRLRRQLAVRRYLAAILGRR”) without haemolytic activity and cytotoxicity displayed enhanced antimicrobial activities against Staphylococcus aureus (S. aureus) ATCC 25923 and Escherichia coli (E. coli) ATCC 25922 than parent VIP even in the presence of 180 mM NaCl or 50 mM MgCl₂, or in the range of pH 4–10. VIP analogue 8 was expressed as fusion protein thioredoxin (Trx)-VIP8 in E. coli BL21(DE) at a yield of 45.67 mg/L. The minimum inhibitory concentration (MIC) of the recombinant VIP analogue 8 against S. aureus ATCC 25923 and E. coli ATCC 25922 were 2 µM. These findings suggest that VIP analogue 8 is a promising candidate for application as a new and safe antimicrobial agent.

Original language	English
Article number	1963
Journal	Molecules
Volume	22
Issue number	11
DOIs	https://doi.org/10.3390/molecules22111963
State	Published - Nov 2017

Keywords

Analogue
Antimicrobial activity
Escherichia coli
Recombinant expression
Vasoactive intestinal peptide

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10.3390/molecules22111963

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title = "Design, recombinant fusion expression and biological evaluation of vasoactive intestinal peptide analogue as novel antimicrobial agent",

abstract = "Antimicrobial peptides represent an emerging category of therapeutic agents with remarkable structural and functional diversity. Modified vasoactive intestinal peptide (VIP) (VIP analogue 8 with amino acid sequence “FTANYTRLRRQLAVRRYLAAILGRR”) without haemolytic activity and cytotoxicity displayed enhanced antimicrobial activities against Staphylococcus aureus (S. aureus) ATCC 25923 and Escherichia coli (E. coli) ATCC 25922 than parent VIP even in the presence of 180 mM NaCl or 50 mM MgCl2, or in the range of pH 4–10. VIP analogue 8 was expressed as fusion protein thioredoxin (Trx)-VIP8 in E. coli BL21(DE) at a yield of 45.67 mg/L. The minimum inhibitory concentration (MIC) of the recombinant VIP analogue 8 against S. aureus ATCC 25923 and E. coli ATCC 25922 were 2 µM. These findings suggest that VIP analogue 8 is a promising candidate for application as a new and safe antimicrobial agent.",

keywords = "Analogue, Antimicrobial activity, Escherichia coli, Recombinant expression, Vasoactive intestinal peptide",

author = "Chunlan Xu and Yu Guo and Xiangjin Qiao and Xiaoya Shang and Weining Niu and Mingliang Jin",

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T1 - Design, recombinant fusion expression and biological evaluation of vasoactive intestinal peptide analogue as novel antimicrobial agent

AU - Xu, Chunlan

AU - Guo, Yu

AU - Qiao, Xiangjin

AU - Shang, Xiaoya

AU - Niu, Weining

AU - Jin, Mingliang

PY - 2017/11

Y1 - 2017/11

N2 - Antimicrobial peptides represent an emerging category of therapeutic agents with remarkable structural and functional diversity. Modified vasoactive intestinal peptide (VIP) (VIP analogue 8 with amino acid sequence “FTANYTRLRRQLAVRRYLAAILGRR”) without haemolytic activity and cytotoxicity displayed enhanced antimicrobial activities against Staphylococcus aureus (S. aureus) ATCC 25923 and Escherichia coli (E. coli) ATCC 25922 than parent VIP even in the presence of 180 mM NaCl or 50 mM MgCl2, or in the range of pH 4–10. VIP analogue 8 was expressed as fusion protein thioredoxin (Trx)-VIP8 in E. coli BL21(DE) at a yield of 45.67 mg/L. The minimum inhibitory concentration (MIC) of the recombinant VIP analogue 8 against S. aureus ATCC 25923 and E. coli ATCC 25922 were 2 µM. These findings suggest that VIP analogue 8 is a promising candidate for application as a new and safe antimicrobial agent.

AB - Antimicrobial peptides represent an emerging category of therapeutic agents with remarkable structural and functional diversity. Modified vasoactive intestinal peptide (VIP) (VIP analogue 8 with amino acid sequence “FTANYTRLRRQLAVRRYLAAILGRR”) without haemolytic activity and cytotoxicity displayed enhanced antimicrobial activities against Staphylococcus aureus (S. aureus) ATCC 25923 and Escherichia coli (E. coli) ATCC 25922 than parent VIP even in the presence of 180 mM NaCl or 50 mM MgCl2, or in the range of pH 4–10. VIP analogue 8 was expressed as fusion protein thioredoxin (Trx)-VIP8 in E. coli BL21(DE) at a yield of 45.67 mg/L. The minimum inhibitory concentration (MIC) of the recombinant VIP analogue 8 against S. aureus ATCC 25923 and E. coli ATCC 25922 were 2 µM. These findings suggest that VIP analogue 8 is a promising candidate for application as a new and safe antimicrobial agent.

KW - Analogue

KW - Antimicrobial activity

KW - Escherichia coli

KW - Recombinant expression

KW - Vasoactive intestinal peptide

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U2 - 10.3390/molecules22111963

DO - 10.3390/molecules22111963

M3 - 文章

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AN - SCOPUS:85035220759

SN - 1420-3049

VL - 22

JO - Molecules

JF - Molecules

IS - 11

M1 - 1963

ER -

Design, recombinant fusion expression and biological evaluation of vasoactive intestinal peptide analogue as novel antimicrobial agent

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Keywords

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