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Advanced Nanomaterials and Biomaterials from Self-Assembling Peptides
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Advanced Nanomaterials and Biomaterials from Self-Assembling Peptides

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

Deadline for manuscript submissions: closed (28 February 2021) | Viewed by 11036

Special Issue Editor

Prof. Dr. Hiroshi Tsutsumi

E-Mail Website
Guest Editor
Tokyo Institute of Technology, School of Life Science and Technology, Tokyo, Japan
Interests: peptide; protein; self-assembling; biomaterial; cell engineering; bioimaging; nanomaterial

Special Issue Information

Dear Colleagues,

In recent decades, self-assembling peptides have attracted a great deal of attention because of their high designability and functionality.  Self-assembling peptides can form various nano- and microstructures, such as fibers, tubes, rods, spheres, vesicles and capsules in organic solvent or aqueous media.  These nanostructures have been widely used to construct nanodevices, organic–inorganic hybrid materials, drug delivery carriers, antibiotics, and artificial extracellular matrices.

This Special Issue will focus on the self-asssembling peptides as nanomaterials and biomaterials.  New entries of self-assembling peptides with various nanostructures and properties are welcomed.  The use of non-natural amino acids and chemical modification of peptides will enrich the variety of self-assembling peptides.  In addition, various applications of self-assembling peptides are expected to benefit the fields of nanotechnology and biotechnology.  For example, self-assembling peptides are potential scaffolds to construct hybrid nanomaterials for optical and electronic devices that involve light harvesting system.  Nanostructures of self-assembling peptides have also received a great deal of attention as scaffolds for mineralization of metallic/inorganic nanomaterials including silica, hydroxyapatite, semiconductor and metal oxides.  In another instance, the assembled structures of designed peptides, such as networked-nanofibers, are expected to be artificial extracellular matrices for cell culture, tissue engineering and regenerative medicine.  Networked-nanofibers form hydrogel materials that can give similar environment to natural hydrogels composed of extracellular matrices.  In addition, biomaterials fabricated from SAPs are also attractive for biomedical applications, such as drug delivery systems and antibacterial materials.

Thus, this Special Issue will widely offer recent advances in self-assembling peptides, from fundamental research to application in nanotechnology and biotechnology.

It is my pleasure to invite you to submit a manuscript for this Special Issue. Full papers, communications, and reviews are all welcome.

Prof. Dr. Hiroshi Tsutsumi
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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. Materials 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 2600 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

  • Peptide
  • Self-assembly
  • Nanostructure
  • Nanomaterial
  • Biomaterial

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Published Papers (3 papers)

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Research

14 pages, 2593 KiB  
Article
Tuning the Photophysical Features of Self-Assembling Photoactive Polypeptides for Light-Harvesting
by Maciej Michalik, Mateusz Zbyradowski, Heriyanto and Leszek Fiedor
Materials 2019, 12(21), 3554; https://doi.org/10.3390/ma12213554 - 30 Oct 2019
Cited by 3 | Viewed by 2709
Abstract
The LH1 complex is the major light-harvesting antenna of purple photosynthetic bacteria. Its role is to capture photons, and then store them and transfer the excitation energy to the photosynthetic reaction center. The structure of LH1 is modular and it cooperatively self-assembles from [...] Read more.
The LH1 complex is the major light-harvesting antenna of purple photosynthetic bacteria. Its role is to capture photons, and then store them and transfer the excitation energy to the photosynthetic reaction center. The structure of LH1 is modular and it cooperatively self-assembles from the subunits composed of short transmembrane polypeptides that reversibly bind the photoactive cofactors: bacteriochlorophyll and carotenoid. LH1 assembly, the intra-complex interactions and the light-harvesting features of LH1 can be controlled in micellar media by varying the surfactant concentration and by adding carotenoid and/or a co-solvent. By exploiting this approach, we can manipulate the size of the assembly, the intensity of light absorption, and the energy and lifetime of its first excited singlet state. For instance, via the introduction of Ni-substituted bacteriochlorophyll into LH1, the lifetime of this electronic state of the antenna can be shortened by almost three orders of magnitude. On the other hand, via the exchange of carotenoid, light absorption in the visible range can be tuned. These results show how in a relatively simple self-assembling pigment-polypeptide system a sophisticated functional tuning can be achieved and thus they provide guidelines for the construction of bio-inspired photoactive nanodevices. Full article
(This article belongs to the Special Issue Advanced Nanomaterials and Biomaterials from Self-Assembling Peptides)
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12 pages, 2184 KiB  
Article
One Step Preparation of Peptide-Coated Gold Nanoparticles with Tunable Size
by Yongmei Jia, Xiaoning Yan, Xin Guo, Guohua Zhou, Peilian Liu and Zhiguo Li
Materials 2019, 12(13), 2107; https://doi.org/10.3390/ma12132107 - 30 Jun 2019
Cited by 21 | Viewed by 4011
Abstract
Gold nanoparticles (AuNPs) made from self-assembling peptides have been used in many research fields and attracted a great deal of attention due to their high stability, biocompatibility and functionality. However, existing preparation methods for peptide-coated AuNPs are post-synthesis processes, which are complicated and [...] Read more.
Gold nanoparticles (AuNPs) made from self-assembling peptides have been used in many research fields and attracted a great deal of attention due to their high stability, biocompatibility and functionality. However, existing preparation methods for peptide-coated AuNPs are post-synthesis processes, which are complicated and time consuming. Therefore, a one-step preparation method for peptide-coated AuNPs is proposed here. The AuNPs obtained by this method exhibit good stability. Importantly, peptide-coated AuNPs with precise different sizes can be prepared by this method through pH control of reducing reagent tyrosine in range of 10.0~12.7. Thus, the one-step preparation method proposed here provides a significant tool for the research in different fields concerning NP size, stability and biocompatibility. Full article
(This article belongs to the Special Issue Advanced Nanomaterials and Biomaterials from Self-Assembling Peptides)
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13 pages, 25599 KiB  
Article
Customized Peptide Biomaterial Synthesis via an Environment-Reliant Auto-Programmer Stigmergic Approach
by Ravindra V. Badhe, Pradeep Kumar, Yahya E. Choonara, Thashree Marimuthu, Lisa C. Du Toit, Divya Bijukumar, Dharmesh R. Chejara, Mostafa Mabrouk and Viness Pillay
Materials 2018, 11(4), 609; https://doi.org/10.3390/ma11040609 - 16 Apr 2018
Cited by 1 | Viewed by 3692
Abstract
Stigmergy, a form of self-organization, was employed here to engineer a self-organizing peptide capable of forming a nano- or micro-structure and that can potentially be used in various drug delivery and biomedical applications. These self-assembling peptides exhibit several desirable qualities for drug delivery, [...] Read more.
Stigmergy, a form of self-organization, was employed here to engineer a self-organizing peptide capable of forming a nano- or micro-structure and that can potentially be used in various drug delivery and biomedical applications. These self-assembling peptides exhibit several desirable qualities for drug delivery, tissue engineering, cosmetics, antibiotics, food science, and biomedical surface engineering. In this study, peptide biomaterial synthesis was carried out using an environment-reliant auto-programmer stigmergic approach. A model protein, α-gliadin (31, 36, and 38 kD), was forced to attain a primary structure with free –SH groups and broken down enzymatically into smaller fragments using chymotrypsin. This breakdown was carried out at different environment conditions (37 and 50 °C), and the fragments were allowed to self-organize at these temperatures. The new peptides so formed diverged according to the environmental conditions. Interestingly, two peptides (with molecular weights of 13.8 and 11.8 kD) were isolated when the reaction temperature was maintained at 50 °C, while four peptides with molecular weights of 54, 51, 13.8, and 12.8 kD were obtained when the reaction was conducted at 37 °C. Thus, at a higher temperature (50 °C), the peptides formed, compared to the original protein, had lower molecular weights, whereas, at a lower temperature (37 °C), two peptides had higher molecular weights and two had lower molecular weights. Full article
(This article belongs to the Special Issue Advanced Nanomaterials and Biomaterials from Self-Assembling Peptides)
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