• structure–activity relationships of αs-casein peptides with multifunctional biological activities

    نویسندگان :
    جزئیات بیشتر مقاله
    • تاریخ ارائه: 1392/07/24
    • تاریخ انتشار در تی پی بین: 1392/07/24
    • تعداد بازدید: 1071
    • تعداد پرسش و پاسخ ها: 0
    • شماره تماس دبیرخانه رویداد: -
     multifunctional bioactive peptides have a wider role in modulating physiological functions and possess multiple biological activities. peptides from bovine milk with sequences qkalneinqf [p10] and tkktklteeeknrl [p14] from α-s2 casein f (79–88) and α-s2 casein f (148–161) were identified to be having multifunctional biological activities and were synthesized. these synthesized peptides show various biological activities like angiotensin-converting enzyme inhibition, prolyl endopeptidase inhibition, antioxidant, and antimicrobial activities. the mode of antimicrobial mechanism was studied and p10 shows depolarization of cell membrane, whereas p14 was found to display dna-binding activity. structural studies envisaged backbone flexibility, for differences in their mode of action. peptide structure function studies were correlated to understand their multifunctional biological activity.

سوال خود را در مورد این مقاله مطرح نمایید :

با انتخاب دکمه ثبت پرسش، موافقت خود را با قوانین انتشار محتوا در وبسایت تی پی بین اعلام می کنم
مقالات جدیدترین رویدادها
مقالات جدیدترین ژورنال ها