Department of Food Science, Institute of Nutrition and Functional Foods (INAF), Université Laval, Quebec, QC G1V 0A6, Canada.
Arla Foods amba, 8200 Aarhus, Denmark.
Molecules. 2021 Mar 6;26(5):1432. doi: 10.3390/molecules26051432.
Self-assembling peptides have gained attention because of their nanotechnological applications. Previous work demonstrated that the self-assembling peptide f1-8 (Pf1-8) that is generated from the tryptic hydrolysis of β-lactoglobulin can form a hydrogel after several purification steps, including membrane filtration and consecutive washes. This study evaluates the impact of each processing step on peptide profile, purity, and gelation capacity of each fraction to understand the purification process of Pf1-8 and the peptide-peptide interactions involved. We showed that peptide-peptide interactions mainly occurred through electrostatic and hydrophobic interactions, influencing the fraction compositions. Indeed, the purity of Pf1-8 did not correlate with the number of wash steps. In addition to Pf1-8, two other hydrophobic peptides were identified, peptide f15-20, and peptide f41-60. The gelation observed could be induced either through peptide-peptide interactions or through self-assembling, both being driven by non-covalent bond and more specifically hydrophobic interactions.
自组装肽因其在纳米技术中的应用而受到关注。以前的工作表明，由β-乳球蛋白的酶解产生的自组装肽 f1-8（Pf1-8）可以在经过几次纯化步骤后形成水凝胶，包括膜过滤和连续洗涤。本研究评估了每个处理步骤对肽谱、每个馏分的纯度和凝胶形成能力的影响，以了解 Pf1-8 的纯化过程和涉及的肽-肽相互作用。我们表明，肽-肽相互作用主要通过静电和疏水相互作用发生，影响馏分组成。实际上，Pf1-8 的纯度与洗涤步骤的数量无关。除了 Pf1-8 之外，还鉴定出另外两种疏水性肽，肽 f15-20 和肽 f41-60。观察到的凝胶化可以通过肽-肽相互作用或自组装诱导，这两种作用都由非共价键驱动，更具体地说是疏水相互作用驱动。
