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Tuesday, July 28, 2020 | History

4 edition of Antimicrobial activity of lactoferrin and lactoferrin derived peptides found in the catalog.

Antimicrobial activity of lactoferrin and lactoferrin derived peptides

Havard Jenssen

Antimicrobial activity of lactoferrin and lactoferrin derived peptides

by Havard Jenssen

  • 324 Want to read
  • 9 Currently reading

Published by Nova Science in Hauppauge, NY .
Written in English

    Subjects:
  • Lactoferrin -- Physiological effect,
  • Lactoferrin -- Derivatives -- Physiological effect,
  • Anti-infective agents,
  • Lactoferrin -- metabolism,
  • Anti-Infective Agents -- metabolism,
  • Antineoplastic Agents -- metabolism

  • Edition Notes

    Includes bibliographical references and index.

    StatementHavard Jenssen.
    Classifications
    LC ClassificationsQP552.L345 J46 2009
    The Physical Object
    Paginationp. ;
    ID Numbers
    Open LibraryOL23055628M
    ISBN 109781606925188
    LC Control Number2009003385

      Therefore, in this case the inhibi- antimicrobial activity than the whole molecule has been tion mechanism exerted by the native proteins may be more widely demonstrated for bovine lactoferrin [8, 16], and eVective than the inhibition exerted by the lactoferrin- some peptides with a great antimicrobial activity have been derived peptides. Keywords:milk, lactoferrin, lactoferricin, lfcin, antimicrobial, peptide, immunomodulation, multifunctional. Abstract: Lactoferricin (LFcin) was initially identified as an antimicrobial peptide derived by pepsin digestion of lactoferrin (LF), a multifunctional innate-defense protein in milk. Various synthetic analogs of LFcin have also been.

    Topics of discussion include antimicrobial activity of lactoferrin and lactoferrin-derived peptides, dietary protein requirements for preterm infants in the neonatal period, antimicrobial activity of lactoferrin and lactoperoxidase in milk, and determination of protein degradability and its importance in ruminant nutrition. lactoferrin receptors of microorganisms are called lactoferrin-binding proteins A and B (LbpA и LbpB) (). The probability of these events increases as the level of free lactoferrin declines but can be cut short by adding its exogenous analog. The second component of the antimicrobial action of lactoferrin is its bactericidal Size: KB.

    The antimicrobial activity of lactoferrin occurs via a high affinity linkage with iron, making this ion unavailable to many bacterial species. It also exerts antimicrobial activity using other mechanisms of action, such as, the direct interaction between lactoferrin and . Milk Derived Peptides with Immune Stimulating Antiviral Properties. By Haiyan Sun and Håvard Jenssen Most studies indicate that lactoferrin and its derived peptides are likely to interfere in the virus host cell Lactoferrampin has been shown to exhibit antimicrobial activity and can improving immune function and gut health in the Cited by: 3.


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Antimicrobial activity of lactoferrin and lactoferrin derived peptides by Havard Jenssen Download PDF EPUB FB2

Antimicrobial Activity of Lactoferrin and Lactoferrin Derived Peptides [Jenssen, Havard] on *FREE* shipping on qualifying offers. Antimicrobial Activity of Lactoferrin and Lactoferrin Derived PeptidesAuthor: Havard Jenssen.

This book examines the antimicrobial, antibacterial, antiviral, antifungal, and antiparasitic activity of lactoferrin (LF), a protein found in mammal milk, and of lactoferricin (LFCIN), an N-terminal pepsin-derived peptide fragment of LF.

The selective activity demonstrated by LF and LFCIN towards tumor cell membranes is also discussed. Abstract. Although the antimicrobial activity of lactoferrin has been well described, its mechanism of action has been poorly characterized.

Recent work has indicated that in addition to binding iron, human lactoferrin damages the outer membrane of gram-negative by: Antimicrobial activity of lactoferrin and lactoferrin derived peptides.

Hauppauge, NY: Nova Science, © (DLC) (OCoLC) Material Type: Document, Internet resource: Document Type: Internet Resource, Computer File: All Authors /. Get this from a library.

Antimicrobial activity of lactoferrin and lactoferrin derived peptides. [Havard Jenssen]. The presence of all these antimicrobial peptides in a single domain of lactoferrin suggests that the protein acts on the membrane interface and disturbs the membrane integrity resulting in its antimicrobial activity.

Since lactoferrin is found in the milk and is ingested throughout the life of all neonates and most adults, it may be an Cited by: Lactoferrin (LF) is a member of the transferrin family that is a cationic iron-binding protein.

It is an kDa glycoprotein that is found in many secretions in the body and is highly present in milk and colostrums. It exerts antibacterial effects and has a wide range of biological activities.

Moreover, it is considered as a precursor of different peptides that have multifunctional : Adham M. Abdou, Hend A. Elbarbary. In this study, synthetic human lactoferrampin (LFampH) peptides were characterized to determine which residues were important for the antimicrobial activity of these related human lactoferrin-derived peptide sequences.

LFampH was modeled after the same region of the LFampB peptide and it corresponds to residues – in human by: Letters in Applied Microbiology26, – Antibacterial activity of bovine lactoferrin and its peptides against enterohaemorrhagic Escherichia coli OH7.

Shin, K. Yamauchi, S. Teraguchi, H. Hayasawa, M. Tomita, Y. Otsuka1 and S. Yamazaki1 Nutritional Science Laboratory, Morinaga Milk Industry Co. Ltd, Zama-City, Kanagawa, and 1Department of. The antimicrobial activity of Lf and one N-terminal peptide fragment of Lf (lactoferricin) are the main topics of this book, with particular focus on antiviral activities.

Antibacterial, –fungal and –parasitic activities are discussed, in addition to the selective activity demonstrated by Lf and lactoferricin, towards tumor cell membranes. Lactoferrin is a multifunctional, iron-binding glycoprotein which displays a wide array of modes of action to execute its primary antimicrobial function.

It contains various antimicrobial peptides which are released upon its hydrolysis by proteases. These peptides display a similarity with the antimicrobial cationic peptides found in nature. In the current scenario of increasing resistance Cited by: Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine Article Literature Review (PDF Available) in Molecules 21(6).

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 Cited by: Free 2-day shipping.

Buy Antimicrobial Activity of Lactoferrin and Lactoferrin Derived Peptides at Lactoferricin and lactoferrampin are two antimicrobial peptides found in the N-terminal lobe of bovine lactoferrin with broad spectrum antimicrobial activity against a. MECHANISMS OF THE ANTIBACTERIAL ACTIVITY OF LACTOFERRIN AND LACTOFERRIN-DERIVED PEPTIDES ANCA ROŞEANU1*, MARIA DAMIAN2, ROBERT W.

EVANS3 1Institute of Biochemistry of the Romanian Academy, Splaiul IndependenţeiBucharest, Romania 2“I. Cantacuzino” National Institute of Research-Development for Microbiology and Immunology. The research of new antimicrobial compounds has an impact on public health and economy of many countries.

Given the great problem of bacterial resistance, the study of new molecules that bypass this mechanism is of great importance. Trypsin is an enzyme necessary for gut physiology and the peptides it forms could be of great interest to the pharmaceutical by: 2. Bovine lactoferrin was hydrolysed with a range of proteolytic enzymes including calf rennet, fungal rennin, and porcine pepsin.

Lactoferrin hydrolysates were assessed for their antibacterial activities against Escherichia coli and Bacillus pH 3, calf rennet lactoferrin hydrolysate before (LFH) showed the highest antimicrobial activity, then pepsin LFH, while fungal rennin LFH was Cited by: portance for the antimicrobial activity, but this is outside the scope of this review.

In addition to antiviral and antibacterial activity, lactoferrin also inhibits fungal [41,42] and parasitic infections [43]. This review provides an overview of the direct antimicrobial functions of the milk protein lactoferrin, namely its antibacterial.

Antibacterial Activity of Lactoferrin and a Pepsin-Derived Lactoferrin Peptide Fragment KOJI YAMAUCHI,12'3 MAMORU TOMITA,1 THEODORE J. GIEHL,2'3t AND RICHARD T. ELLISON III2,3t* Medical and Research Services, Department of Veterans Affairs Medical Center,2 and Division of Infectious Diseases, Department ofMedicine.

Antimicrobial peptides representing this domain were isolated following pepsin cleavage of human lactoferrin and bovine lactoferrin. The antimicrobial sequence was found to consist mainly of a loop of 18 amino acid residues formed by a disulfide bond between cysteine residues 20 and 37 of human lactoferrin, or 19 and 36 of bovine by: Lactoferrin (LF), also known as lactotransferrin (LTF), is a multifunctional protein of the transferrin family.

Lactoferrin is a globular glycoprotein with a molecular mass of about 80 kDa that is widely represented in various secretory fluids, such as milk, saliva, tears, and nasal errin is also present in secondary granules of PMNs and is secreted by some Aliases: LTF, GIG12, HEL, HLF2, LF.

phils [ ]. It exerts a wide antimicrobial activity against a numberofbacterial,viral,andfungalpathogensinvitro[ ]. Lactoferrin exerts its antimicrobial action not just in the form of the intact molecule but the monoferric lobes and active peptides of lactoferrin also have a role in theCited by: