Peptide Conjugates for Biological Applications
The conjugation of peptide and protein holds a prominent position in the field of bioconjugate chemistry, which has great potentials in the biomedical area, and undergoes intensive research for years. The paper highlights several significant activities regarding this technology.
Novel approaches of peptide and protein functionalization have been discovered in recent years by creative scientists. Deming described modification strategies for methionine in his review. Ozer and Chilkoti described a selective modification of therapeutic peptides and proteins that combines the expertise of molecular biology, organic and polymer chemistry, with the aim of controlling over conjugation. The significance of site selective control is subsequently described by Klok and his colleagues' review about conjugating different PEG architectures to a peptide heptad repeat fusion inhibitor against HIV-1. Their successful full control over the site of attachment enabled them to study the structure-activity relationship systematically. The Heilshorn group adopted tyrosine modification as a site selective tool, which furth made contributions in cell culture. All the above-mentioned studies prove the significant value of bioconjugation chemistry's application in biomedical areas.
The second sector illustrates the peptide conjugates with super-molecular features, especially the peptide-based amphiphiles, which is led in by the review of Hamley and Castelletto. Guler and colleagues demonstrated how a fiber-based hydrogel is made from the modular assembly of different peptide amphiphiles. Furthermore, the versatility of the peptide amphiphile approach was further proved by incorporating a tetrathiophene unit, and functional fibers were formed that can be used to support the differentiation of neural stem cells.
In the third section, the applications of peptide conjugates in drug delivery are introduced based on various research papers. Borner et al. reported that the peptide conjugates can be used as solubilizing agents for drugs that are poorly water-soluble. And with a combined method, they successfully obtained the sequence information for several photosensitizers. Regarding the peptide-mediated oligonucleotide delivery to cells, Lehto demonstrated a cell penetrating peptide modified with a fatty acid tail that allows complexation with the oligonucleotide to be delivered, and in Astakhova's paper, by click chemistry, an oligonucleotide−peptide conjugate was developed and meanwhile its effect on the antisense oligonucleotides properties was studied. Lu gave an example of peptide motifs' importance.
The last part is mainly around protein conjugates. Under such conditions, the selective modification of specific site is more challenging than that of peptide. Protein conjugation can improve properties, but may cut down the binding efficacy. Maynard and partners researched on a polymer conjugated with trehalose side chains that can improve certain properties of therapeutic proteins, to which was then paid attention to on the aspect of controlled synthesis by Ovaa and Kiick et al. Rodriguez Cabello and co-workers developed a facile protein engineering approach to construct ELPs with FRET properties. At the end of this special issue, a paper of Brock about using currently available 3D tissue models to take a deeper look at peptide and protein behaviors in a biomimetic environment.
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