Synthetic macromolecular peptide-mimetics with amino acid substructure residues as protein stabilising excipients

文献情報

出版日 2023-12-29

DOI 10.1039/D3TB02102E

インパクトファクター 6.331

著者

Ruggero Foralosso, Cameron Alexander, Giuseppe Mantovani, Snow Stolnik

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要旨

The clinical use of protein and peptide biotherapeutics requires fabrication of stable products. This particularly concerns stability towards aggregation of proteins or peptides. Here, we tested a hypothesis that interactions between a synthetic peptide, which is an aggregation-prone region analogue, and its homologous sequence on a protein of interest, could be exploited to design excipients which stabilise the protein against aggregation. A peptide containing the analogue of lysozyme aggregation-prone region (GILQINSRW) was conjugated to a RAFT agent and used to initiate the polymerisation of N-hydroxyethyl acrylamide, generating a GILQINSRW-HEA90 polymer, which profoundly reduced lysozyme aggregation. Substitution of tryptophan in GILQINSRW with glycine, to form GILQINSRG, revealed that tryptophan is a critical amino acid in the protein stabilisation by GILQINSRW-HEA90. Accordingly, polymeric peptide-mimetics of tryptophan, phenylalanine and isoleucine, which are often present in aggregation-prone regions, were synthesized. These were based on synthetic oligomers of acrylamide derivatives of indole-3 acetic acid (IND), phenylacetic acid (PHEN), or 2-methyl butyric acid (MBA), respectively, conjugated with hydrophilic poly(N-hydroxyethyl acrylamide) blocks to form amphiphilic copolymers denoted as INDm-, PHENm- and MTBm-b-HEAn. These materials were tested as protein stabilisers and it was shown that solution properties and the abilities of these materials to stabilise insulin and the peptide IDR 1018 towards aggregation are dependent on the chemical nature of their side groups. These data suggest a structure–activity relationship, whereby the indole-based INDm-b-HEAn peptide-mimetic displays properties of a potential stabilising excipient for protein formulations.

掲載誌

Journal of Materials Chemistry B

CiteScore: 12

自己引用率: 4.9%

年間論文数: 831

Journal of Materials Chemistry A, B & C cover high quality studies across all fields of materials chemistry. The journals focus on those theoretical or experimental studies that report new understanding, applications, properties and synthesis of materials. The journals have a strong history of publishing quality reports of interest to interdisciplinary communities and providing an efficient and rigorous service through peer review and publication. The journals are led by an international team of Editors-in-Chief and Associate Editors who are all active researchers in their fields. Journal of Materials Chemistry A, B & C are separated by the intended application of the material studied. Broadly, applications in energy and sustainability are of interest to Journal of Materials Chemistry A, applications in biology and medicine are of interest to Journal of Materials Chemistry B, and applications in optical, magnetic and electronic devices are of interest to Journal of Materials Chemistry C. More than one Journal of Materials Chemistry journal may be suitable for certain fields and researchers are encouraged to submit their paper to the journal that they feel best fits for their particular article. Example topic areas within the scope of Journal of Materials Chemistry B are listed below. This list is neither exhaustive nor exclusive. Antifouling coatings Biocompatible materials Bioelectronics Bioimaging Biomimetics Biomineralisation Bionics Biosensors Diagnostics Drug delivery Gene delivery Immunobiology Nanomedicine Regenerative medicine & Tissue engineering Scaffolds Soft robotics Stem cells Therapeutic devices image block All articles published in Journal of Materials Chemistry B from 2019 onwards will be indexed in MEDLINE®. Articles that primarily focus on providing insight into the underlying science and performance of biomaterials within a biological environment are more suited to our companion journal, Biomaterials Science.

Synthetic macromolecular peptide-mimetics with amino acid substructure residues as protein stabilising excipients

文献情報

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Journal of Materials Chemistry B

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