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Journal ArticleDOI

Identification of the bactericidal domain of lactoferrin.

TLDR
The studies suggest this domain is the structural region responsible for the bacterial properties of lactoferrin, having effectiveness against various Gram-negative and Gram-positive bacteria at concentrations between 0.3 microM and 3.0 microM, depending on the target strain.
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This article is published in Biochimica et Biophysica Acta.The article was published on 1992-05-22. It has received 882 citations till now. The article focuses on the topics: Lactoferricin & Lactoferrin.

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Citations
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Journal ArticleDOI

Studies on anticancer activities of antimicrobial peptides.

TL;DR: Various studies on different cationic antimicrobial peptides that exhibit cytotoxic activity against cancer cells are reviewed and the suitability of cancer cell-targeting AMPs as cancer therapeutics is discussed.
Journal ArticleDOI

Anti-microbial peptides: from invertebrates to vertebrates

TL;DR: This review focuses on AMPs forming α‐helices, β‐hairpin‐like β‐sheets, α‐helix/β‐sheet mixed structures from invertebrate and vertebrate origins, which show some promise for therapeutic use.
Journal ArticleDOI

Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action.

TL;DR: In this review, the structures of a number of different Trp- and Arg-rich antimicrobial peptides are examined and some of the major mechanistic studies are presented.
Journal Article

Antimicrobial activity of

TL;DR: A method using scanning electron microscope to study the morphology of the bacterial and fungal microbes and thus determining antimicrobial activity is presented in the chapter.
Journal ArticleDOI

Lactoferrin: molecular structure and biological function.

TL;DR: Lactoferrin has been proposed to play a role in iron uptake by the intestinal mucosa and to act as a bacteriostatic agent by withholding iron from iron-requiring bacteria.
References
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Journal ArticleDOI

Killing of gram-negative bacteria by lactoferrin and lysozyme.

TL;DR: Dialysis chamber studies indicate that bacterial killing requires direct contact with lactoferrin, and work with purified LPS suggests that this relates to direct LPS-binding by the protein, suggesting that their interaction contributes to host defense.
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A bactericidal effect for human lactoferrin

TL;DR: Streptococcus mutans and Vibrio cholerae, but not Escherichia coli, were killed by incubation with purified human apolact oferrin, contingent upon the metal-chelating properties of the lactoferrin molecule.
Journal ArticleDOI

An iron-binding protein common to many external secretions

TL;DR: The iron-binding protein characteristic of milk, here called lactoferrin, has been demonstrated to occur in saliva, nasal secretions, tears, bronchial mucus, hepatic bile, pancreatic juice, seminal fluid, female cervical mucus and urines and it is suggested that it is of value in the defence of epithelial surfaces against infection.
Journal ArticleDOI

Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2·8 Å resolution

TL;DR: The structure of human lactoferrin has been refined crystallographically at 2.8 A (1 A = 0.1 nm) resolution using restrained least squares methods, and details of the secondary structure and tertiary interactions have been clarified.
Journal ArticleDOI

Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins

TL;DR: The complete amino acid sequence (703 amino acid residues) of human lactotransferrin has been determined and prediction of the secondary structure of the two homologous moieties of human dairy product has been performed.
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