We have investigated the potential of bile acid (BA)-binding short-chain peptides for suppressing cholesterol absorption in the intestine. In our previous report, we have revealed the physicochemical characteristics of high binding peptides using principal component analysis. In this study, we investigated the characteristics of amino acid residues of BA-binding short-chain peptides. We found that short-chain peptides containing lysine (K) and arginine (R) had a higher BA-binding ability than peptides containing other amino acids. Since short-chain tryptic peptides contain K or R residues, we focused on 4-mer, 5-mer, and 6-mer peptides, which were expectedly released from the edible proteins by trypsin. Forty-four short-chain peptides from lactoproteins (Bos taurus) and glutelin (Oryza sativa subsp. Japonica) were synthesized, and their BA micelle disruption activity was evaluated. We could observe such activities in nearly all tested peptides. We found that CEVFR, NGLK, and NSVFR had particularly high disruption activities. We determined that the 50% cholesterol concentration decrease value (DC50) of the micellar solution upon peptide addition was almost the same in case of the aforementioned peptides as that of the VAWWMY as a positive control. In addition, 4-mer and 5-mer peptides had higher BA micelle disruption activity than 6-mer peptides. Our results confirmed that the BA binding and micelle disruption activities were significantly higher if the short-chain peptides contained K and R residues.

我们已经研究了胆汁酸（BA）结合短链肽抑制肠道胆固醇吸收的潜力。在我们以前的报告中，我们使用主成分分析揭示了高结合肽的理化特性。在这项研究中，我们调查了BA结合短链肽的氨基酸残基的特征。我们发现，含有赖氨酸（K）和精氨酸（R）的短链肽比含有其他氨基酸的肽具有更高的BA结合能力。由于短链胰蛋白酶解肽含有K或R残基，因此我们重点研究了4聚体，5聚体和6聚体肽，这些肽有望通过胰蛋白酶从可食用蛋白质中释放出来。来自乳蛋白（Bos taurus）和谷蛋白（Oryza sativa）的四十四个短链肽亚种 合成了粳稻，并评估了它们的BA胶束破坏活性。我们几乎可以在所有测试的肽中观察到这种活性。我们发现CEVFR，NGLK和NSVFR具有特别高的破坏活性。我们确定，在上述肽的情况下，添加肽时胶束溶液的50％胆固醇浓度降低值（DC50）与作为阳性对照的VAWWMY几乎相同。另外，4聚体和5聚体的肽比6聚体的肽具有更高的BA胶束破坏活性。我们的结果证实，如果短链肽含有K和R残基，则BA结合和胶束破坏活性明显更高。