Analisi in silico di caseinofosfopeptidi (CFP) nei ruminanti

In silico analysis of caseinophosphopeptides in ruminants. - Milk proteins are the main source of bioactive peptides with different functions. These milk activities are hidden in the native proteins and require the proteolitic cleavage to become extrinsic. The biopeptides generated from milk protein digestion show a wide range of activities. On the basis of the effects induced in the organism, biopeptides can be classified in the following categories: opioid-agonist, opioid-antagonist, antihypertensive, antithrombotic, immunomodulatory, antimicrobial, and mineral carrier peptides. These last peptides, also called caseinophosphopeptides (CPPs), possess the ability to bind and solubilise minerals, such as Ca2+. Consumption of high concentrations of Ca2+ in early life contributes to the development of maximal bone density, which in turn can prevent osteoporosis in later life. Furthermore, a positive correlation was found between Ca2+ intake and the prevention of hypertension. The high bioavailability of Ca2+ from milk and dairy products has, in part, been attributed to the production of CPPs with different levels of phosphorylation. The studies on the biological effect of different CPPs were carried out mainly in the bovine species, without taking genetic polymorphism into account. The biological activity of peptides released from milk protein digestion may be affected by aminoacid exchanges or deletions resulting from gene mutations, as well as by prost-translational changes. The aim of this work was to carry out an in silico analysis of the CPPs in order to detect differences in the aminoacid sequence among species (bovine, caprine, and ovine) and the genetic variants within each species. We analysed 3, 2, and 3 CPPs respectively carried by alphaS1-casein (CSN1S1), beta-casein (CSN2), and alphaS2-casein (CSN1S2). The biological effects of these peptides, or fragments of them, are known from literature. A total of 30 differences were detected when comparing the bovine, caprine, and ovine species as well as the genetic variants within each species. Among the most interesting variations we can focus on: i. the deletion of peptide 59-78 in the goat CSN1S1*F variant, which is rather common in most caprine breeds; ii. the lost of a phosphorylated serine within peptide 29-41 in the bovine CSN2*C variant, which is the fourth beta-casein variant, in order of frequency, in cattle; iii. the lost of a phosphorylated serine within peptide 1-21 in the bovine CSN1S2*B variant, mainly spread in Bos indicus but also found in some Bos taurus breeds

Milk proteins are the main source of bioactive peptides with different functions. These milk activities are hidden in the native proteins and require the proteolitic cleavage to become extrinsic. The biopeptides generated from milk protein digestion show a wide range of activities. On the basis of the effects induced in the organism, biopeptides can be classified in the following categories: opioid-agonist, opioid-antagonist, antihypertensive, antithrombotic, immunomodulatory, antimicrobial, and mineral carrier peptides. These last peptides, also called caseinophosphopeptides (CPPs), possess the ability to bind and solubilise minerals, such as Ca2+. Consumption of high concentrations of Ca2+ in early life contributes to the development of maximal bone density, which in turn can prevent osteoporosis in later life. Furthermore, a positive correlation was found between Ca2+ intake and the prevention of hypertension. The high bioavailability of Ca2+ from milk and dairy products has, in part, been attributed to the production of CPPs with different levels of phosphorylation. The studies on the biological effect of different CPPs were carried out mainly in the bovine species, without taking genetic polymorphism into account. The biological activity of peptides released from milk protein digestion may be affected by aminoacid exchanges or deletions resulting from gene mutations, as well as by prost-translational changes. The aim of this work was to carry out an in silico analysis of the CPPs in order to detect differences in the aminoacid sequence among species (bovine, caprine, and ovine) and the genetic variants within each species.We analysed 3, 2, and 3 CPPs respectively carried by alphaS1-casein (CSN1S1), beta-casein (CSN2), and alphaS2-casein (CSN1S2). The biological effects of these peptides, or fragments of them, are known from literature. A total of 30 differences were detected when comparing the bovine, caprine, and ovine species as well as the genetic variants within each species. Among the most interesting variations we can focus on: i. the deletion of peptide 59-78 in the goat CSN1S1*F variant, which is rather common in most caprine breeds; ii. the lost of a phosphorylated serine within peptide 29-41 in the bovine CSN2*C variant, which is the fourth beta-casein variant, in order of frequency, in cattle; iii. the lost of a phosphorylated serine within peptide 1-21 in the bovine CSN1S2*B variant, mainly spread in Bos indicus but also found in some Bos taurus breeds