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Review
. 2016 Jun 11;21(6):752.
doi: 10.3390/molecules21060752.

Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine

Natascia Bruni  1 , Maria Teresa Capucchio  2 , Elena Biasibetti  3 , Enrica Pessione  4 , Simona Cirrincione  5 , Leonardo Giraudo  6 , Antonio Corona  7 , Franco Dosio  8
Affiliations
Review

Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine

Natascia Bruni et al. Molecules. .

Abstract

Antimicrobial peptides (AMPs) represent a vast array of molecules produced by virtually all living organisms as natural barriers against infection. Among AMP sources, an interesting class regards the food-derived bioactive agents. The whey protein lactoferrin (Lf) is an iron-binding glycoprotein that plays a significant role in the innate immune system, and is considered as an important host defense molecule. In search for novel antimicrobial agents, Lf offers a new source with potential pharmaceutical applications. The Lf-derived peptides Lf(1-11), lactoferricin (Lfcin) and lactoferrampin exhibit interesting and more potent antimicrobial actions than intact protein. Particularly, Lfcin has demonstrated strong antibacterial, anti-fungal and antiparasitic activity with promising applications both in human and veterinary diseases (from ocular infections to osteo-articular, gastrointestinal and dermatological diseases).

Keywords: antimicrobial peptides; food safety; lactoferricin; milk proteins.

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Conflict of interest statement

Candioli Farmaceutici is the funding sponsor in writing the manuscript.

Figures

Figure 1
Figure 1
Overall structure of lactoferrin showing positions of the functional peptides Lf(1–11) (red), lactoferrampin (pink), and lactoferricin (blue) in the N-terminal lobe.
Figure 2
Figure 2
Structure of Lf(1–11) peptide.
Figure 3
Figure 3
Structure of Lfcin peptide.
Figure 4
Figure 4
Structure of Lfampin.
See this image and copyright information in PMC

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