Controlling gelation with sequence: Towards programmable peptide hydrogels.

Area of Science:

• Biomaterials Science
• Peptide Engineering
• Nanotechnology

Background:

• Self-assembling peptides are valuable for creating biocompatible and biodegradable bionanomaterials.
• The peptide IKHLSVN, inspired by protein-protein interfaces, represents a new class of bio-inspired peptides.

Purpose of the Study:

• To characterize the self-assembly of the peptide IKHLSVN (dubbed littleSven) and its modified sequences.
• To investigate the resilience of the peptide sequence to self-assembly and hydrogel formation.
• To explore how minor sequence alterations impact hydrogel properties for diverse applications.

Main Methods:

• Characterization of the parent peptide and its modified analogues.
• Systematic modification of the IKHLSVN sequence (side chain and N-terminus).
• Assessment of self-assembly behavior, hydrogel formation, and material properties (gelation time, rheology, gel strength).

Main Results:

• The parent peptide IKHLSVN did not form a hydrogel.
• Minor modifications (single side chain or N-terminus) induced hydrogel formation.
• Altered sequences resulted in tunable hydrogel properties, including gelation time and rheology.
• Modifications influenced amyloid-like characteristics and gel strength.

Conclusions:

• Peptides derived from protein-protein interfaces demonstrate sequence resilience for hydrogel formation.
• Small, targeted modifications can effectively tune the properties of self-assembling peptides.
• Engineered peptides offer a versatile platform for developing advanced bionanomaterials with controlled characteristics.