Self-assembling short oligopeptides and the promotion of angiogenesis

Peptide conjugate hydrogelators

“…Recent results show that, at a concentration of 14.6 mM, the hydrophobicity of the Fmocdipeptides determines whether a gel will form at pH 4. 148 Fmoc- 15 dipeptides with a logP (a measure of the hydrophobicity) lower than 2.4 form gels that synerise, those with a logP between 2.4 and 5.5 form stable gels and Fmoc-PhePhe (logP = 5.6) does not form a gel at this pH, in agreement with other results. A number of recent reports from the Ulijn group have demonstrated that gelation can also be induced and controlled by enzymatic-triggered assembly.…”

“…Supramolecular hydrogels prepared using these forces have properties which are very different to those arising from 15 cross-linked polymer hydrogels. Since the matrix is held together by non-covalent interaction, the gels tend to have rapid response to chemical or physical stimuli such as pH and temperature.…”

“…The C-terminus end of the peptide chain is anchored to a solid support resin, 10 which leaves the N-terminus end free to react with the free Cterminus of an N-terminus protected amino acid in solution (in excess). Following removal of the protecting group on the Nterminus of the resin-based peptide, the next solution-based peptide can be introduced or, alternatively, the peptide 15 sequence can be cleaved from the solid resin, which is filtered off to afford the final product in extremely high yield. Each step is quasi-quantitative, but cumulative steps result in lower final yields.…”

“…Monohydroxy PEO 7 was converted to PEO 7 -N 3 and 10 subsequently reacted with an alkyne-modified PhePhePhePhe moiety (synthesised by solution phase amino acid coupling) with 73 % click efficiency. Pegylation, the coupling of PEO to peptides or proteins, is a well-studied field (due to the biocompatibility of PEO and its effect in prolonging the 15 lifetime of biological compounds in the body) and is reviewed in detail elsewhere. For PA synthesis, alkylation is generally achieved by standard amidation following peptide construction.…”

Peptide-based biopolymers in biomedicine and biotechnology

“…Zhang et al have synthesized short oligopeptides having 12 to 16 amino acids that spontaneously form stable β-sheet structures under physiological solution conditions [220][221][222][223][224][225][226][227][228][229][230][231][232][233][234][235]. As shown in Figure 19a, these ionic selfcomplementary oligopeptides have amphiphilic character; one face of the molecule consists of nonpolar, hydrophobic amino acids (such as Ala, Phe, or Leu), and the other face consists of alternating oppositely charged amino acids (such as positively charged Lys or Arg and negatively charged Asp or Glu).…”