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Polymers
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Polypeptide Containing Polymers
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Polypeptide Containing Polymers

A special issue of Polymers (ISSN 2073-4360).

Deadline for manuscript submissions: closed (25 March 2018)

Special Issue Editor

Prof. Dr. Hermis Iatrou

E-Mail Website
Guest Editor
Department of Chemistry, University of Athens, Panepistimiopolis, Zografou, 15771 Athens, Greece
Interests: polymer synthesis; nanomedicine; drug and gene delivery; polypeptides; well-defined polymers; macromolecular architecture; ring-opening polymerization of N-carboxy anhydrides; biopolymers; nanotechnology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Synthetic polymers can be obtained from many monomers, in miscellaneous architectures, including, not only linear, but also branched systems, through "living" polymerization techniques. However, none of these polymers exhibit the sophistication and complexity of those derived from the combination of only 20 amino acids, i.e., polypeptides, that can self-organize mainly through physical forces in length scales, from a few angstroms to a few microns, to achieve the required functionality. Polypeptides present the 3D structures found in natural proteins, such as α-helices and β-sheets, that renders these materials "smart". Synthetic polypeptides have the advantage of being composed of much simpler components than natural proteins, but do not present the complex biological activity of a protein. However, due to their 3D structure and biocompatibility, polypeptides have become the most promising materials in many bio-applications, such as drug and gene delivery. In addition, the combination of polypeptides with synthetic biocompatible conventional polymers could lead to the formation of nanoconstructs with sophisticated higher-order structures with new properties and functionalities. Consequently, polypeptide-containing polymers are very interesting materials that attract the interest of an increasing number of scientists in a variety of disciplines.

This Special Issue is intended to highlight the synthesis and applications of polypeptide containing polymers, for instance stimuli-responsive/smart materials, hierarchical structures, self-organization, biomedical applications, and others.

Prof. Hermis Iatrou
Guest Editor

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Polymers is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Polypeptides
  • N-Carboxy Anhydrides
  • Bio-Inspired polymers
  • Hybrids
  • Biomaterials
  • Drug Delivery
  • Anticancer Agents
  • Cancer
  • Stimuli Responsive materials
  • Smart Materials
  • Hierarchical Organization

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Published Papers (5 papers)

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Research

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12 pages, 10002 KiB  
Article
KnowVolution of the Polymer-Binding Peptide LCI for Improved Polypropylene Binding
by Kristin Rübsam, Mehdi D. Davari, Felix Jakob and Ulrich Schwaneberg
Polymers 2018, 10(4), 423; https://doi.org/10.3390/polym10040423 - 10 Apr 2018
Cited by 56 | Viewed by 7992
Abstract
The functionalization of polymer surfaces by polymer-binding peptides offers tremendous opportunities for directed immobilization of enzymes, bioactive peptides, and antigens. The application of polymer-binding peptides as adhesion promoters requires reliable and stable binding under process conditions. Molecular modes of interactions between material surfaces, [...] Read more.
The functionalization of polymer surfaces by polymer-binding peptides offers tremendous opportunities for directed immobilization of enzymes, bioactive peptides, and antigens. The application of polymer-binding peptides as adhesion promoters requires reliable and stable binding under process conditions. Molecular modes of interactions between material surfaces, peptides, and solvent are often not understood to an extent that enables (semi-) rational design of polymer-binding peptides, hindering the full exploitation of their potential. Knowledge-gaining directed evolution (KnowVolution) is an efficient protein engineering strategy that facilitates tailoring protein properties to application demands through a combination of directed evolution and computational guided protein design. A single round of KnowVolution was performed to gain molecular insights into liquid chromatography peak I peptide, 47 aa (LCI)-binding to polypropylene (PP) in the presence of the competing surfactant Triton X-100. KnowVolution yielded a total of 8 key positions (D19, S27, Y29, D31, G35, I40, E42, and D45), which govern PP-binding in the presence of Triton X-100. The recombination of two of the identified amino acid substitutions (Y29R and G35R; variant KR-2) yielded a 5.4 ± 0.5-fold stronger PP-binding peptide compared to LCI WT in the presence of Triton X-100 (1 mM). The LCI variant KR-2 shows a maximum binding capacity of 8.8 ± 0.1 pmol/cm2 on PP in the presence of Triton X-100 (up to 1 mM). The KnowVolution approach enables the development of polymer-binding peptides, which efficiently coat and functionalize PP surfaces and withstand surfactant concentrations that are commonly used, such as in household detergents. Full article
(This article belongs to the Special Issue Polypeptide Containing Polymers)
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15 pages, 15651 KiB  
Article
The Length of Hydrophobic Chain in Amphiphilic Polypeptides Regulates the Efficiency of Gene Delivery
by Ying Zhang, Zhiping Zhou and Mingsheng Chen
Polymers 2018, 10(4), 379; https://doi.org/10.3390/polym10040379 - 1 Apr 2018
Cited by 19 | Viewed by 7939
Abstract
The major challenges of non-viral carriers are low transfection efficiency and high toxicity. To overcome this bottleneck, it is very important to investigate the structure-property-function (transfection efficiency) relationships of polycations. Herein, different length hydrophobic poly(l-leucine) chains in amphiphilic polypeptides were precisely [...] Read more.
The major challenges of non-viral carriers are low transfection efficiency and high toxicity. To overcome this bottleneck, it is very important to investigate the structure-property-function (transfection efficiency) relationships of polycations. Herein, different length hydrophobic poly(l-leucine) chains in amphiphilic polypeptides were precisely synthesized by α-amino acid N-carboxyanhydrides (NCA) ring-opening polymerization and these biocompatible polypeptides were chosen as a model to further examine the transfection in vitro. These polypeptides were characterized by nuclear magnetic resonance spectroscopy (NMR) and size exclusion chromatography (SEC). Agarose gel electrophoresis (AGE) was employed to validate the ability of DNA condensation and transmission electron microscopy (TEM) was used to observe the assemblies of polyplexes. Cytotoxicity was evaluated in COS-7 cell lines and transfection was performed in normal cell COS-7 and cancer cell Hep G2. The results showed that NCA monomers were prepared and the amphiphilic polypeptides, poly(lysine(CBZ))50-block-poly(l-leucine)10, poly(l-lysine(CBZ))50-block-poly(l-leucine)15, and poly(l-lysine(CBZ))50-block-poly(l-leucine)25, were successfully synthesized with controlled molecular weight and narrow distribution. After deprotection of CBZ, these materials can condense plasmid DNA into 100 nm nanoparticles and the cellular uptake of polyplexes was as fast as 30 min. The transfection data shown these materials had a good transfection efficiency comparing to polyethylenimine (Branched, 25 kDa) while they displayed ignored cytotoxicity. More importantly, we discovered the length of hydrophobic poly(l-leucine) in amphiphilic polypeptides steadily regulates gene delivery efficiency in two kinds of cells ranking poly(l-lysine)50-block-poly(l-leucine)25 > poly(l-lysine)50-block-poly(l-leucine)15 > poly(l-lysine)50-block-poly(l-leucine)10. Full article
(This article belongs to the Special Issue Polypeptide Containing Polymers)
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5133 KiB  
Article
Synthesis of Hybrid-Polypeptides m-PEO-b-poly(His-co-Gly) and m-PEO-b-poly(His-co-Ala) and Study of Their Structure and Aggregation. Influence of Hydrophobic Copolypeptides on the Properties of Poly(L-histidine)
by Dimitrios Skoulas, Dimitra Stavroulaki, Konstantinos Santorinaios and Hermis Iatrou
Polymers 2017, 9(11), 564; https://doi.org/10.3390/polym9110564 - 30 Oct 2017
Cited by 9 | Viewed by 6178
Abstract
The highly diverse and sophisticated action of proteins results from their equally diverse primary structure, which along with the nature of interactions between the amino acids, defines the higher self-assembly of proteins. The interactions between amino acids can be very complicated, and their [...] Read more.
The highly diverse and sophisticated action of proteins results from their equally diverse primary structure, which along with the nature of interactions between the amino acids, defines the higher self-assembly of proteins. The interactions between amino acids can be very complicated, and their understanding is necessary in order to elucidate the protein structure-properties relationship. A series of well-defined hybrid-polypeptidic diblock copolymers of the type m-PEO-b-poly(His-co-Gly) and m-PEO-b-poly(His-co-Ala) was synthesized through the ring opening polymerization of the N-carboxyanhydrides of the corresponding amino acids, with a molar ratio of the hydrophobic peptide to histidine at 10%, 20% and 40%. The excellent purity of the monomers combined with the high vacuum techniques resulted in controlled polymerization with high molecular and compositional homogeneity. FT-IR, as well as circular dichroism, were employed to investigate the secondary structure of the polymers, while DLS, SLS and ζ-potential were utilized to study the aggregates formed in aqueous solutions, as well as their pH responsiveness. The results revealed that the randomly distributed monomeric units of glycine or alanine significantly influence L-histidine’s structure. Depending on the pH, aggregates with a different structure, different molecular characteristics and a different surface charge are formed, potentially leading to very interesting bioapplications. Full article
(This article belongs to the Special Issue Polypeptide Containing Polymers)
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3143 KiB  
Article
Smart Poly(imidazoyl-l-lysine): Synthesis and Reversible Helix-to-Coil Transition at Neutral pH
by Estefania Piedra-Arroni, Fatma Makni, Laura Severac, Jean-Luc Stigliani, Geneviève Pratviel and Colin Bonduelle
Polymers 2017, 9(7), 276; https://doi.org/10.3390/polym9070276 - 11 Jul 2017
Cited by 13 | Viewed by 9813
Abstract
Polypeptide polymers can adopt natural protein secondary structures such as α-helices or β-sheets, and this unique feature is at the origin of some intriguing physico–chemical properties. In this work, we present how side chain imidazoylation of a poly(l-lysine) scaffold affords the [...] Read more.
Polypeptide polymers can adopt natural protein secondary structures such as α-helices or β-sheets, and this unique feature is at the origin of some intriguing physico–chemical properties. In this work, we present how side chain imidazoylation of a poly(l-lysine) scaffold affords the preparation of poly(histidine) counterparts exhibiting α-helix conformation. This structuring behavior is reversible and can be controlled by means of pH and or temperature changes. Full article
(This article belongs to the Special Issue Polypeptide Containing Polymers)
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Review

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21760 KiB  
Review
Strategies to Fabricate Polypeptide-Based Structures via Ring-Opening Polymerization of N-Carboxyanhydrides
by Carmen M. González-Henríquez, Mauricio A. Sarabia-Vallejos and Juan Rodríguez-Hernández
Polymers 2017, 9(11), 551; https://doi.org/10.3390/polym9110551 - 25 Oct 2017
Cited by 35 | Viewed by 14261
Abstract
In this review, we provide a general and clear overview about the different alternatives reported to fabricate a myriad of polypeptide architectures based on the ring-opening polymerization of N-carbonyanhydrides (ROP NCAs). First of all, the strategies for the preparation of NCA monomers [...] Read more.
In this review, we provide a general and clear overview about the different alternatives reported to fabricate a myriad of polypeptide architectures based on the ring-opening polymerization of N-carbonyanhydrides (ROP NCAs). First of all, the strategies for the preparation of NCA monomers directly from natural occurring or from modified amino acids are analyzed. The synthetic alternatives to prepare non-functionalized and functionalized NCAs are presented. Protection/deprotection protocols, as well as other functionalization chemistries are discussed in this section. Later on, the mechanisms involved in the ROP NCA polymerization, as well as the strategies developed to reduce the eventually occurring side reactions are presented. Finally, a general overview of the synthetic strategies described in the literature to fabricate different polypeptide architectures is provided. This part of the review is organized depending on the complexity of the macromolecular topology prepared. Therefore, linear homopolypeptides, random and block copolypeptides are described first. The next sections include cyclic and branched polymers such as star polypeptides, polymer brushes and highly branched structures including arborescent or dendrigraft structures. Full article
(This article belongs to the Special Issue Polypeptide Containing Polymers)
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