Occurrence of Peptide-Peptide Interactions during the Purification of Self-Assembling Peptide f1-8 from a ß-Lactoglobulin Tryptic Hydrolysate.
Molecules
; 26(5)2021 Mar 06.
Article
in En
| MEDLINE
| ID: mdl-33800800
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 ß-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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptide Fragments
/
Hydrogels
/
Lactoglobulins
Language:
En
Journal:
Molecules
Journal subject:
BIOLOGIA
Year:
2021
Document type:
Article
Affiliation country:
Canadá