Abstract
In-silico study was carried out to study motifs present in precursors of antimicrobial, antithrombotic, casein derived and mineral binding bioactive peptides by using online servers. MEME suite was used for defining the common consensus pattern present in bioactive peptides precursors. It was found that although three different consensus patterns was identified in precursors but theses consensus pattern overlapped in many sequences and all three motifs may be present in many peptides precursor sequences.
Highlights
Bioactive peptides have been defined as specific protein fragments that have a positive impact on body functions and conditions and may influence health 1
Most of the bioactivities of bioactive peptides are encrypted within the primary sequence of the native protein and peptides require to be released through one of the following ways: Hydrolysis by digestive enzymes such as trypsin and pepsin [5, 7], Food processing 6 and Through hydrolysis by proteolytic microorganisms or through the action of proteolytic enzymes derived from the microorganisms 4
We found that consensus pattern present in motif three belongs to the opioid peptides precursor seq no [32, 27, 26, 34, 14] and 30
Summary
Bioactive peptides have been defined as specific protein fragments that have a positive impact on body functions and conditions and may influence health 1. Jolles et al, (1986) 8 showed that bovine kcasein f106-116 inhibited platelet aggregation and combined with the receptor site, preventing fibrinogen binding with blood platelets. The two smaller tryptic peptides (k-casein f106-112 and f113-116) exerted a much more minimal effect on platelet aggregation and did not inhibit fibrinogen binding These peptides are referred to as casoplatelins. The κ-casein fragment named casoplatelins, obtained from tryptic hydrolysates, shows antithrombotic activity by inhibiting fibrinogen binding platelets [9,10]. These peptides are released during gastrointestinal digestion and absorbed intact into the blood, which supports the concept that they exert an antithrombotic effect in vivo. The potential physiological effects of these antithrombotic peptides have not been
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