Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 103, Issue 23-24, Pages 9607-9618Publisher
SPRINGER
DOI: 10.1007/s00253-019-10187-5
Keywords
ENTEROCIN CRL35; MICROCIN V; HYBRID PEPTIDE; HINGE REGION; MUTAGENESIS; ANTIMICROBIAL ACTIVITY
Categories
Funding
- Agencia Nacional de Promocion Cientifica y Tecnologica (ANPCyT) [PICT 4610]
- Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET) [PIP 06906 CO]
- Secretaria de Ciencia, Arte e Innovacion Tecnologica (SCAIT) from Universidad Nacional de Tucuman (UNT) [PIUNT D641/1]
- CONICET fellowship
- ANPCyT fellowship
Ask authors/readers for more resources
The present paper describes the generation of derivatives from the hybrid peptide called Ent35-MccV, active against Gram-positive and Gram-negative bacteria. This peptide has a triple glycine hinge region between enterocin CRL35 and microcin V. In order to obtain variants of Ent35-MccV with greater biotechnological potential, a saturation mutagenesis was carried out in the hinge region. As a result, we obtained a bank of E. coli strains expressing different mutated hybrid bacteriocins in the central position of the hinge region. From all these variants, we found that the one bearing a tyrosine in the central region of the hinge (Ent35-GYG-MccV) is 2-fold more active against E. coli and 4-fold more active against Listeria than the original peptide Ent35-MccV. This derivative was purified and characterized. The development and evaluation of alternative hinges for Ent35-MccV represents a step forward in the bioengineering of antimicrobial peptides. This approach fosters the rational design of peptides with enhanced antimicrobial activity.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available