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Synthetic Protein Mimics: Advances in Architectures and Applications

A special issue of Materials (ISSN 1996-1944). This special issue belongs to the section "Polymeric Materials".

Deadline for manuscript submissions: closed (20 September 2023) | Viewed by 4361

Special Issue Editors


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Guest Editor
Department of Polymer Science and Engineering, Zhejiang University, Hangzhou 310027, China
Interests: living/controlled polymerization methodologies; catalysis and rare earth metal catalysts; synthesis of polymers with complex topologies; design and application of functional polymeric materials; Monte Carlo simulation in polymer science; quantum chemical calculation and molecular modeling

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Guest Editor
School of Materials Science and Engineering, East China University of Science and Technology, Shanghai 200237, China
Interests: living/controlled polymerization methodologies; functional poly(amino acid)s; photo-responsive polymers; polymer self-assembly; polymeric biomaterials; hydrogels

Special Issue Information

Dear Colleagues,

As synthetic mimics of natural proteins, poly(α-amino acid)s (also known as polypeptides), poly(N-substituted-α-amino acid)s (also known as polypeptoids), poly(β-amino acid)s, polyoxazolines, polyoxazine, etc., are attractive biomaterials with excellent biocompatibility and degradability due to their similar structures to proteins. Their synthetic methods have been continuously developed in recent years. Thanks to the development of characterization and excellent experimental works, some old mechanism questions also see the dawn of lights. The synthetic methods mainly include biosynthesis, solid-phase synthesis, ring-opening polymerizations (ROPs) of various monomers. Taking polypeptides and polypeptoids as examples, the ROPs of N-carboxyanhydride and N-thiocarboxyanhydride have the advantages of simple operation, low cost, living/controlled characteristics and high molecular weight of products, which have brought great opportunities for the applications of protein mimicking materials.

Chiral centers and multiple hydrogen bond interactions along the backbones allow the peptide-containing polymers to form secondary structures, such as α-helix and β-sheet, for constructing precisely ordered biofunctional nanomaterials. Their properties, including hydrophilicity, hydrophobicity, (bio)degradability and bioactivity, can be easily tuned by changing the architectures of backbones and functional side groups, as well as the copolymerization with other polymers. They have been extensively applied in the fields of drug delivery, nucleic acid and protein delivery, biomedicine, bioimaging, cell scaffolds, etc.

This Special Issue will compile recent developments in the field of synthesis, characterization and applications of various synthetic mimics of proteins. The articles presented in this Special Issue will cover various topics, ranging from but not limited to the novel synthetic methods of ROPs and polycondensations, solid-phase synthesis, functional side chain design, polymerization mechanism, macromolecular architecture, novel property study, self-assembly, hydrogels, surface modification and various biomedical applications. Topics are open to synthetic methods, macromolecular architectures and biomedical applications of such promising materials.

Prof. Dr. Jun Ling
Dr. Xinfeng Tao
Guest Editors

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Keywords

  • biomaterials
  • biomedical applications
  • secondary structure
  • self-assembly
  • poly(amino acid)s
  • polypeptides
  • polypeptoids
  • polyoxazonlines
  • polyoxazines

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Published Papers (2 papers)

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Research

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11 pages, 3214 KiB  
Article
Zwitterionic Polypeptoids: A Promising Class of Antifouling Bioinspired Materials
by Jian Ding, Xiangmin Ding and Jing Sun
Materials 2022, 15(13), 4498; https://doi.org/10.3390/ma15134498 - 26 Jun 2022
Cited by 3 | Viewed by 1712
Abstract
Biofouling caused by protein adsorption and microbial colonization remains a great challenge in many applications. In this work, we synthesized a new type of zwitterionic polypeptoid containing carboxybetaine (CB) moieties (PeptoidCB) through thiol–ene chemistry of poly(N-allylglycine) (PNAG). The zwitterionic antifouling hydrogel was subsequently [...] Read more.
Biofouling caused by protein adsorption and microbial colonization remains a great challenge in many applications. In this work, we synthesized a new type of zwitterionic polypeptoid containing carboxybetaine (CB) moieties (PeptoidCB) through thiol–ene chemistry of poly(N-allylglycine) (PNAG). The zwitterionic antifouling hydrogel was subsequently prepared by co-mixing PeptoidCB with agarose, which exhibited excellent resistance to non-specific protein adsorption and bacterial adhesion. Further, PeptoidCB-modified block copolypeptoids with amphiphilic structure were synthesized to form nanoparticles in an aqueous solution with neglected protein adsorption. The ability of PeptoidCB to resist non-specific protein adsorption and bacterial adhesion makes it a promising candidate for biomedical and industrial applications. Full article
(This article belongs to the Special Issue Synthetic Protein Mimics: Advances in Architectures and Applications)
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Review

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21 pages, 5985 KiB  
Review
Recent Experimental Advances in Characterizing the Self-Assembly and Phase Behavior of Polypeptoids
by Liying Kang, Qi Wang, Lei Zhang, Hang Zou, Jun Gao, Kangmin Niu and Naisheng Jiang
Materials 2023, 16(11), 4175; https://doi.org/10.3390/ma16114175 - 3 Jun 2023
Cited by 1 | Viewed by 2098
Abstract
Polypeptoids are a family of synthetic peptidomimetic polymers featuring N-substituted polyglycine backbones with large chemical and structural diversity. Their synthetic accessibility, tunable property/functionality, and biological relevance make polypeptoids a promising platform for molecular biomimicry and various biotechnological applications. To gain insight into the [...] Read more.
Polypeptoids are a family of synthetic peptidomimetic polymers featuring N-substituted polyglycine backbones with large chemical and structural diversity. Their synthetic accessibility, tunable property/functionality, and biological relevance make polypeptoids a promising platform for molecular biomimicry and various biotechnological applications. To gain insight into the relationship between the chemical structure, self-assembly behavior, and physicochemical properties of polypeptoids, many efforts have been made using thermal analysis, microscopy, scattering, and spectroscopic techniques. In this review, we summarize recent experimental investigations that have focused on the hierarchical self-assembly and phase behavior of polypeptoids in bulk, thin film, and solution states, highlighting the use of advanced characterization tools such as in situ microscopy and scattering techniques. These methods enable researchers to unravel multiscale structural features and assembly processes of polypeptoids over a wide range of length and time scales, thereby providing new insights into the structure–property relationship of these protein-mimetic materials. Full article
(This article belongs to the Special Issue Synthetic Protein Mimics: Advances in Architectures and Applications)
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