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Improved Antimicrobial Activity of Bovine Lactoferrin Peptide (LFcinB) Based on Rational Design

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Abstract

Bovine lactoferrin peptide (LFcinB), as an antimicrobial peptide, is expected to be an alternative of antibiotics owing to its broad-spectrum antimicrobial activity and specific mechanism. However, the weak antimicrobial activity, high hemolysis, and poor stability of LFcinB limited its applications in the field of biomedicine, food and agriculture. In order to improve the antimicrobial activity of LFcinB, five mutants were designed rationally, of which mutant LF4 (M10W/P16R/A24L) showed highest antimicrobial activity. The bioinformatics analysis indicated that the improved antimicrobial activity of LF4 was related to its increased cations, higher amphiphilicity and the extension of the β-sheet in the structure. These studies will highlight the important role of bioinformatic tools in designing ideal biopeptides and lay a foundation for further development of antimicrobial peptides.

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Acknowledgements

We thank to the financial support of the National Natural Science Foundation of China (No. 22208058) to B. S.

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  1. College of Biological Science and Engineering, Fuzhou University, Fuzhou, 350116, Fujian, China

    Xiaokun Hong, Xueqian Liu, Bingmei Su & Juan Lin

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J. L. conceived the study; X. L. collected the data; X. L. and X. H. analyzed the data; X. H. and B. S. drafted the manuscript; All authors edited and approved the final version of the manuscript.

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Correspondence to Bingmei Su or Juan Lin.

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Hong, X., Liu, X., Su, B. et al. Improved Antimicrobial Activity of Bovine Lactoferrin Peptide (LFcinB) Based on Rational Design. Protein J 42, 633–644 (2023). https://doi.org/10.1007/s10930-023-10142-4

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