title: Modification of β-Sheet Forming Peptide Hydrophobic Face: Effect on Self-Assembly and Gelation.
abstract: β-Sheet forming peptides have attracted significant interest for the design of hydrogels for biomedical applications. One of the main challenges is the control and understanding of the correlations between peptide molecular structure, the morphology, and topology of the fiber and network formed as well as the macroscopic properties of the hydrogel obtained. In this work, we have investigated the effect that functionalizing these peptides through their hydrophobic face has on their self-assembly and gelation. Our results show that the modification of the hydrophobic face results in a partial loss of the extended β-sheet conformation of the peptide and a significant change in fiber morphology from straight to kinked. As a consequence, the ability of these fibers to associate along their length and form large bundles is reduced. These structural changes (fiber structure and network topology) significantly affect the mechanical properties of the hydrogels (shear modulus and elasticity).
authors.forename: Mohamed A
authors.initials: MA
authors.lastname: Elsawy
authors.forename: Andrew M
authors.initials: AM
authors.lastname: Smith
authors.forename: Nigel
authors.initials: N
authors.lastname: Hodson
authors.affiliation: Department of Chemistry, Reading University , Whiteknights RG6 6AD, Reading, U.K.
authors.forename: Adam
authors.initials: A
authors.lastname: Squires
authors.forename: Aline F
authors.initials: AF
authors.lastname: Miller
authors.forename: Alberto
authors.initials: A
authors.lastname: Saiani
mesh_terms: D000595:Amino Acid Sequence; D005782:Gels; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D000072757:Protein Conformation, beta-Strand
chemical_list: D005782:Gels; D010455:Peptides