Current Pharmaceutical Design - Volume 9, Issue 16, 2003

Antimicrobial peptides are present in men, animals and plants and represent an important component of the innate immunity. Nevertheless they can also be generated through proteolytical digestion of food proteins. Thus, food proteins can be regarded not only for their nutritive value but also as a possible resource to increase the natural defence of the organism against invading pathogens. Consequently food proteins can Read More

Mammary fluids, colostrum and milk, deliver nature's first host defense systems upon birth, and these essential liquids are critical for survival of the neonate. The identification and characterization of anti-infectious proteins were among the early scientific discoveries and this group of proteins has long been recognized for promoting health benefits in both newborns and adults. Among the more widely studied are the immunogl Read More

Milk forms a rich source of biologically interesting components. In particular, its protein fraction is known to encompass many kinds of biological functions. In this review we focus on antibacterial and antiviral properties of milk proteins and milk protein derivatives. The latter include chemically modified proteins and enzymatically induced peptides. If such peptides are released by enzymes present within the digestive tract (e.g. t Read More

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 reported. LFcin inhibits a diverse range of microorganisms such as gram-negative bacteria, gram-positive bacteria, yeast, filamentous fungi, and parasitic protozoa, including some antibiotic-resistant pathogen Read More

The protein fraction of milk contains many valuable components and biologically active substances. Moreover, milk proteins are precursors of many different biologically active peptides which are inactive within the sequence of the precursor protein but can be released by enzymatic proteolysis. Many milk protein-derived peptides, such as caseinophosphopeptides, reveal multifunctional bioactivities. Caseinophosphop Read More

Dietary proteins are known to carry a wide range of nutritional, functional and biological properties. Nutritionally, the proteins are a source of energy and amino acids, which are essential for growth and maintenance. Functionally, the proteins contribute to the physicochemical and sensory properties of various protein-rich foods. Furthermore, many dietary proteins possess specific biological properties which make these co Read More

There are many examples of biologically active food proteins, with physiological significance beyond the pure nutritional requirements that concern available nitrogen for normal growth and maintenance. Moreover, there are many physiologically active peptides, derived by protease activity from various food protein sources; however, relationships between structural properties and functional activities have not been completely el Read More

Opioid peptides showing selectivity for d receptor have been isolated from enzymatic digests of plant proteins. Five peptides were derived from wheat gluten, and named gluten exorphins A5, A4, B5, B4 and C. Two opioid peptides were also released from spinach ribulosebisphosphate- carboxylase / oxygenase (Rubisco), and named rubiscolins-5 and -6. Among them, gluten exorphin 5A (Gly-Tyr-Tyr-Pro-Thr) and rubiscolin Read More

During the last two decades a variety of food protein fragments has been demonstrated to elicit biological effects in various in vitro or in vivo test systems. A considerable part of these bioactive peptides are opioid receptor ligands , which may be regarded as exogenous supplements to the endogenous opioidergic systems of the human organism. Most of these foodderived opioid receptor ligands are fragments of the milk pr Read More

This paper reviews bioactive peptides, biogenic peptides, opioid peptides, immunostimulating peptides, mineral soluble peptides, antihypertensive peptides and antimicrobial peptides originating from food materials and enzymatic hydrolysis of proteins. Antihypertensive peptides are extensively reviewed and have been divided into angiotensin Iconverting enzyme inhibitory peptides and others. These peptides are produced in the Read More