Occurrence of Peptide-Peptide Interactions during the Purification of Self-Assembling Peptide f1-8 from a β-Lactoglobulin Tryptic Hydrolysate.

Mathilde Pimont-Farge,Alain Doyen,Yves Pouliot,Shyam Suwal,Véronique Perreault,Guillaume Brisson,Amélie Bérubé

doi:10.3390/molecules26051432

Mathilde Pimont-Farge, Alain Doyen + Show 5 more

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https://doi.org/10.3390/molecules26051432

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Abstract

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.

Highlights

The enzymatic hydrolysis of whey proteins has been extensively studied to reduce the allergenicity of bovine proteins [1], as well as to generate bioactive peptides [2] and innovative ingredients with functional properties [3,4]
Of these 50 components, 24 peptide sequences that were generated from tryptic hydrolysis of β-lactoglobulin and the peak corresponding to α-lactalbumin were identified in the hydrolysate, according to the peptide profiles that were reported by Pouliot et al [25] using an identical method (Figure 1a)
Our results showed the similarities between the peptide profiles of the initial βlactoglobulin tryptic hydrolysates and the fractions that were obtained after filtration experiments (UFr and ROr as well as UFp) (Figure 1)

Summary

Introduction

The enzymatic hydrolysis of whey proteins has been extensively studied to reduce the allergenicity of bovine proteins [1], as well as to generate bioactive peptides [2] and innovative ingredients with functional properties [3,4]. The self-assembling properties of peptides have garnered increased interest in the last few years due to their applications in tissue regeneration, drug delivery, biosensors, and immunotherapy [7]. This process of self-assembly corresponds to the ability of a molecule to form highly ordered structures (micelles, vesicles, nanotubes, nanofibers, and hydrogels) through non-covalent interactions, such as hydrophobic and electrostatic interactions, as well as hydrogen bonding [8,9,10,11,12,13,14,15,16]

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