Department of Studies in Biotechnology, University of Mysore, Manasagangotri, Mysore 570 006, Karnataka, India.
Eur J Med Chem. 2012 Jul;53:211-9. doi: 10.1016/j.ejmech.2012.03.057. Epub 2012 Apr 6.
β-lactoglobulin is a rich source of bioactive peptides. The LC-MS separated tryptic peptides of buffalo colostrum β-lactoglobulin (BLG-col) were computed based on MS-MS fragmentation for de novo sequencing. Among the selected peptides (P1-P8), a variant was detected with methionine at position 74 instead of glutamate. The sequences of two peptides were identical to hypocholesterolemic peptides whereas the remaining peptides were in accordance with buffalo milk β-lactoglobulin. Comparative sequence analysis of BLG-col to milk β-lactoglobulin was carried out using CLUSTALW2 and a molecular model for BLG-col was constructed (PMDB ID-PM0076812). The synthesized variant pentapeptide (IIAMK, m/z-576 Da) was found to inhibit angiotensin I-converting enzyme (ACE) with an IC(50) of 498 ± 2 μM, which was rationalized through docking simulations using Molgrow virtual docker.
β-乳球蛋白是生物活性肽的丰富来源。基于 MS-MS 碎片的计算，从水牛初乳β-乳球蛋白（BLG-col）的 LC-MS 分离的胰蛋白酶肽被用于从头测序。在所选择的肽（P1-P8）中，检测到一个变体，其 74 位的谷氨酸被蛋氨酸取代。两个肽的序列与降胆固醇肽相同，而其余肽与水牛乳β-乳球蛋白一致。使用 CLUSTALW2 对 BLG-col 与乳β-乳球蛋白进行比较序列分析，并构建了 BLG-col 的分子模型（PMDB ID-PM0076812）。合成的五肽变体（IIAMK，m/z-576 Da）被发现可抑制血管紧张素 I 转换酶（ACE），其 IC50 为 498±2 μM，这通过使用 Molgrow virtual docker 进行对接模拟得到了合理化。
