β-casein f(54-59) [id=CAB0002]

Producer Organism : Native Protein : Production Method :
Human β-casein Synthetic
Activity : Not determined
Target Organisms :

Unavailable data

Description :
Production method: Synthetic.

Activity in vivo against Klebsiella pneumonia
Length : 6 Mass (Da): 716.87 Common Amino Acids : P
Isolectric Point : 3.85 Net Charge : -1 Absent Amino Acids : ACDFGHKLMNQRSTW
Basic Residues : 0 Acidic Residues : 1 Hydrophobic Residues : 2
Polar Residues : 1 Boman Index : 2.01 Hydropathy Index : 0.117
Aliphatic Index : 113.33 Instability Index : 0 Extinction Coefficient : 1490
Absorbance 280nm : 298

Wheel representation

Hydrophobicity plot

Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).
Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).
Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

Citation: 1

Biodefense properties of milk: The role of antimicrobial proteins and peptides

Cited Entries: CAK0002, CAB0002

Authors:Clare, D.A., Catignani, G.L., Swaisgood, H.E.
Journal: Current Pharmaceutical Design 2003, 9.
Abstract: 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 immunoglobulins, lactoperoxidase, lysozyme, and lactoferrin. Recently, it was shown that alpha--lactalbumin may also function in a protective capacity dependent upon its folding state. Some of these, especially lactoferrin, also display an immunomodulatory role in which case a totally separate cascade of host defense responses is initiated. It was noted that the mechanism of action for this cluster of sentry proteins does vary; thus, this protective strategy provides for a broad range of responsive reactions to infection. Presently, there is a major focus on the discovery of novel peptides that can be generated from existing milk proteins via proteolytic reactions. To date, this substrate list includes alpha--lactalbumin, beta-lactoglobulin, all casein fractions, and lactoferrin. Again, the immunoregulatory effects prompted as a result of the appearance of these peptides are currently being defined. Herein, we review the principal biological properties associated with each of these contributing milk components with a special emphasis on the role of biodefensive milk peptides. We envision future contributions emerging from this research field as an opportunity to develop effective new therapies to be used in treating infectious diseases and promoting health benefits in vivo.
Keywords: milk proteins; peptides; Immunology; a-Lactalbumin; antimicrobial milk proteins; b-lactoglobulin; immunoglobulins; immunoregulatory milk peptides; Lactoferrin; lactoperoxidase
Citation: 2

Immunostimulating hexapeptide from human casein: amino acid sequence, synthesis and biological properties

Cited Entries: CAB0002

Authors:Parker, F., Migliore-Samour, D., Floch, F., Zerial, A., Werner, G.H., Jolles, J., Casaretto, M., Zahn, H., Jolles, P.
Journal: European Journal of Biochemistry 1984, 145(3).
Abstract: A hexapeptide obtained from human casein by enzymatic digestion has been purified, sequenced and synthesized; its structure is: Val-Glu-Pro-Ile-Pro-Tyr. In vitro this hexapeptide stimulates the phagocytosis of opsonized sheep red blood cells by murine peritoneal macrophages. Administered intravenously to adult mice, it enhances the resistance to infection with Klebsiella pneumoniae.

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