Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin.

TL;DR: Clinical studies on the treatment of infectious diseases have been performed with artificial peptides derived from human lactoferrin, histatins and BPI in addition to porcine protegrins, frog magains and bovine indolicidin, showing increasing evidence that AMPs play a crucial role in human immunity.

TL;DR: Powerful new research tools are radically modifying the prospects for the understanding of the interplay between the mammary gland innate defenses and mastitis-causing bacteria: genetic dissection of the immune response, microarray gene technology, transcriptomic methodologies and gene silencing by RNA interference will make possible the discovery of several of the key defense mechanisms which govern the susceptibility/resistance to mastitis at the molecular and genetic levels.

TL;DR: Small cationic antimicrobial peptides, e.g. defensins, cathelicidin and the histatins, have come into focus and are potentially suited as templates for the design of a new generation of antibiotics, since they kill a broad spectrum of microorganisms, while hardly evoking resistance, in contrast to the classical antibiotics.

TL;DR: An outline of the bioactive peptides identified in the muscle protein of meat to date is presented, with a focus on muscle protein from domestic animals and fish.

TL;DR: In this article, the authors defined the mean helical hydrophobic moment, which is defined as the sum of the hydrophobicity of the side chains of a helix of N residues, and reported that trans-membrane helices, which seek surfaces between aqueous and non-polar phases, cluster in different regions of such a plot.

TL;DR: Interactions with lipid bilayers of magainins and tachyplesins discovered in frog skin and horseshoe crab hemolymph are summarized, emphasizing that the mode of interaction is strongly dependent on the physicochemical properties not only of the peptide, but also of the target membrane.

TL;DR: 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.

TL;DR: The observation that many protein sequences tend to form segments of maximum amphiphilicity suggests that segments of secondary structure fold at a hydrophobic surface, probably formed from other parts of the folding protein.