胃肠道内源性蛋白质作为生物活性肽的来源——一项计算机模拟研究
Gastrointestinal endogenous proteins as a source of bioactive peptides--an in silico study.
作者信息
Dave Lakshmi A, Montoya Carlos A, Rutherfurd Shane M, Moughan Paul J
机构信息
Riddet Institute, Massey University, Palmerston North, New Zealand.
出版信息
PLoS One. 2014 Jun 5;9(6):e98922. doi: 10.1371/journal.pone.0098922. eCollection 2014.
Dietary proteins are known to contain bioactive peptides that are released during digestion. Endogenous proteins secreted into the gastrointestinal tract represent a quantitatively greater supply of protein to the gut lumen than those of dietary origin. Many of these endogenous proteins are digested in the gastrointestinal tract but the possibility that these are also a source of bioactive peptides has not been considered. An in silico prediction method was used to test if bioactive peptides could be derived from the gastrointestinal digestion of gut endogenous proteins. Twenty six gut endogenous proteins and seven dietary proteins were evaluated. The peptides present after gastric and intestinal digestion were predicted based on the amino acid sequence of the proteins and the known specificities of the major gastrointestinal proteases. The predicted resultant peptides possessing amino acid sequences identical to those of known bioactive peptides were identified. After gastrointestinal digestion (based on the in silico simulation), the total number of bioactive peptides predicted to be released ranged from 1 (gliadin) to 55 (myosin) for the selected dietary proteins and from 1 (secretin) to 39 (mucin-5AC) for the selected gut endogenous proteins. Within the intact proteins and after simulated gastrointestinal digestion, angiotensin converting enzyme (ACE)-inhibitory peptide sequences were the most frequently observed in both the dietary and endogenous proteins. Among the dietary proteins, after in silico simulated gastrointestinal digestion, myosin was found to have the highest number of ACE-inhibitory peptide sequences (49 peptides), while for the gut endogenous proteins, mucin-5AC had the greatest number of ACE-inhibitory peptide sequences (38 peptides). Gut endogenous proteins may be an important source of bioactive peptides in the gut particularly since gut endogenous proteins represent a quantitatively large and consistent source of protein.
已知膳食蛋白质含有在消化过程中释放的生物活性肽。分泌到胃肠道中的内源性蛋白质向肠腔提供的蛋白质数量比膳食来源的蛋白质更多。这些内源性蛋白质中的许多在胃肠道中被消化，但这些蛋白质也是生物活性肽来源的可能性尚未得到考虑。使用一种计算机预测方法来测试生物活性肽是否可以从肠道内源性蛋白质的胃肠道消化中产生。评估了26种肠道内源性蛋白质和7种膳食蛋白质。根据蛋白质的氨基酸序列和主要胃肠道蛋白酶的已知特异性，预测胃和肠道消化后存在的肽。鉴定出预测的所得肽具有与已知生物活性肽相同的氨基酸序列。在胃肠道消化后（基于计算机模拟），所选膳食蛋白质预测释放的生物活性肽总数范围为1（麦醇溶蛋白）至55（肌球蛋白），所选肠道内源性蛋白质为1（促胰液素）至39（粘蛋白-5AC）。在完整蛋白质和模拟胃肠道消化后，血管紧张素转换酶（ACE）抑制肽序列在膳食和内源性蛋白质中最常被观察到。在膳食蛋白质中，经过计算机模拟胃肠道消化后，发现肌球蛋白具有最高数量的ACE抑制肽序列（49个肽），而对于肠道内源性蛋白质，粘蛋白-5AC具有最多数量的ACE抑制肽序列（38个肽）。肠道内源性蛋白质可能是肠道中生物活性肽的重要来源，特别是因为肠道内源性蛋白质代表了数量上大且一致的蛋白质来源。
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