Effect of Physicochemical Conditions on Peptide−Peptide Interactions in a Tryptic Hydrolysate of β-Lactoglobulin and Identification of Aggregating Peptides

2003 ◽  
Vol 51 (15) ◽  
pp. 4370-4375 ◽  
Author(s):  
Paule Emilie Groleau ◽  
Pierre Morin ◽  
Sylvie F. Gauthier ◽  
Yves Pouliot
Keyword(s):  
Physicochemical Conditions ◽  
Peptide Interactions ◽  
Tryptic Hydrolysate ◽  
Β Lactoglobulin

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

Molecules ◽  
2021 ◽  
Vol 26 (5) ◽  
pp. 1432
Author(s):  
Mathilde Pimont-Farge ◽  
Amélie Bérubé ◽  
Véronique Perreault ◽  
Guillaume Brisson ◽  
Shyam Suwal ◽  
...  
Keyword(s):  
Membrane Filtration ◽  
Hydrophobic Interactions ◽  
Covalent Bond ◽  
Peptide Profile ◽  
Hydrophobic Peptides ◽  
Self Assembling ◽  
Peptide Interactions ◽  
Tryptic Hydrolysate ◽  
The Impact ◽  
Β Lactoglobulin

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.

Selective separation of cationic peptides from a tryptic hydrolysate of β-lactoglobulin by electrofiltration

2006 ◽  
Vol 94 (2) ◽  
pp. 223-233 ◽  
Author(s):  
Jean-François Lapointe ◽  
Sylvie F. Gauthier ◽  
Yves Pouliot ◽  
Christian Bouchard
Keyword(s):  
Selective Separation ◽  
Cationic Peptides ◽  
Tryptic Hydrolysate ◽  
Β Lactoglobulin

Interactions between Bovine β-Lactoglobulin and Peptides under Different Physicochemical Conditions

2002 ◽  
Vol 50 (6) ◽  
pp. 1587-1592 ◽  
Author(s):  
Isabelle Noiseux ◽  
Sylvie F. Gauthier ◽  
Sylvie L. Turgeon
Keyword(s):  
Physicochemical Conditions ◽  
Β Lactoglobulin
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