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9.4
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Biomolecules
Special Issues
Peptides and Proteins as Innovative Biomaterials
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Peptides and Proteins as Innovative Biomaterials

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biomacromolecules: Proteins".

Deadline for manuscript submissions: closed (31 March 2021) | Viewed by 10915

Special Issue Editors

Dr. Anna Tinti

E-Mail Website
Guest Editor
Dipartimento di Scienze Biomediche e Neuromotorie, Alma Mater Studiorum Universita di Bologna, Bologna, Italy
Interests: protein secondary and tertiary structure; protein interaction with metal ions; amphiphilic oligopeptides; biomimetic coatings for biomedical devices; inorganic and organic biomaterials; drug polymorphs characterization; vibrational spectroscopy
Dr. Michele Di Foggia

E-Mail Website
Guest Editor
Department of Biomedical and Neuromotor Sciences, University of Bologna, Via Belmeloro 8/2, 40126 Bologna, Italy
Interests: protein secondary and tertiary structure; protein interaction with metal ions; biomimetic coatings for biomedical devices; vibrational spectroscopy; SERS; tissue engineering; silk fibroin
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Proteins are the biomolecules characterized by the broadest variety of functions, thanks to the different chemical properties of their amino acid building blocks. As a consequence, proteins have been investigated for decades in order to obtain innovative biomaterials, and research has found many biomedical applications (e.g., drug delivery systems, biosensors, and scaffolds for tissue regeneration). In this context, this Special Issue intends to give a general overview of the potential of protein-based biomaterials, covering aspects ranging from biomimetic surfaces to the use of materials of natural origin alone or in composites.

We welcome the submission of original manuscripts and reviews dealing with the synthesis, purification, or spectroscopic characterization of protein biomaterials, together with in vitro and in vivo evaluations of their functionality.

Dr. Anna Tinti
PD Dr. Michele Di Foggia
Guest Editors

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. Biomolecules is an international peer-reviewed open access monthly 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

  • Peptides
  • Proteins
  • Innovative biomaterials
  • Biomedical applications
  • Spectroscopic characterization
  • In vitro and in vivo evaluation
  • Biomimetic materials
  • Protein adsorption
  • Biocompatibility
  • Scaffolds
  • Tissue Engineering

Published Papers (4 papers)

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Research

12 pages, 3419 KiB  
Article
Effects of the Blending Ratio on the Design of Keratin/Poly(butylene succinate) Nanofibers for Drug Delivery Applications
by Giulia Guidotti, Michelina Soccio, Edoardo Bondi, Tamara Posati, Giovanna Sotgiu, Roberto Zamboni, Armida Torreggiani, Franco Corticelli, Nadia Lotti and Annalisa Aluigi
Biomolecules 2021, 11(8), 1194; https://doi.org/10.3390/biom11081194 - 12 Aug 2021
Cited by 22 | Viewed by 2771
Abstract
In recent years there has been a growing interest in the use of proteins as biocompatible and environmentally friendly biomolecules for the design of wound healing and drug delivery systems. Keratin is a fascinating protein, obtainable from several keratinous biomasses such as wool, [...] Read more.
In recent years there has been a growing interest in the use of proteins as biocompatible and environmentally friendly biomolecules for the design of wound healing and drug delivery systems. Keratin is a fascinating protein, obtainable from several keratinous biomasses such as wool, hair or nails, with intrinsic bioactive properties including stimulatory effects on wound repair and excellent carrier capability. In this work keratin/poly(butylene succinate) blend solutions with functional properties tunable by manipulating the polymer blending ratios were prepared by using 1,1,1,3,3,3-hexafluoroisopropanol as common solvent. Afterwards, these solutions doped with rhodamine B (RhB), were electrospun into blend mats and the drug release mechanism and kinetics as a function of blend composition was studied, in order to understand the potential of such membranes as drug delivery systems. The electrophoresis analysis carried out on keratin revealed that the solvent used does not degrade the protein. Moreover, all the blend solutions showed a non-Newtonian behavior, among which the Keratin/PBS 70/30 and 30/70 ones showed an amplified orientation ability of the polymer chains when subjected to a shear stress. Therefore, the resulting nanofibers showed thinner mean diameters and narrower diameter distributions compared to the Keratin/PBS 50/50 blend solution. The thermal stability and the mechanical properties of the blend electrospun mats improved by increasing the PBS content. Finally, the RhB release rate increased by increasing the keratin content of the mats and the drug diffused as drug-protein complex. Full article
(This article belongs to the Special Issue Peptides and Proteins as Innovative Biomaterials)
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20 pages, 7560 KiB  
Article
SERS Investigation on Oligopeptides Used as Biomimetic Coatings for Medical Devices
by Michele Di Foggia, Vitaliano Tugnoli, Stefano Ottani, Monica Dettin, Annj Zamuner, Santiago Sanchez-Cortes, Daniele Cesini and Armida Torreggiani
Biomolecules 2021, 11(7), 959; https://doi.org/10.3390/biom11070959 - 29 Jun 2021
Cited by 5 | Viewed by 2765
Abstract
The surface-enhanced Raman scattering (SERS) spectra of three amphiphilic oligopeptides derived from EAK16 (AEAEAKAK)2 were examined to study systematic amino acid substitution effects on the corresponding interaction with Ag colloidal nanoparticles. Such self-assembling molecular systems, known as “molecular Lego”, are of particular [...] Read more.
The surface-enhanced Raman scattering (SERS) spectra of three amphiphilic oligopeptides derived from EAK16 (AEAEAKAK)2 were examined to study systematic amino acid substitution effects on the corresponding interaction with Ag colloidal nanoparticles. Such self-assembling molecular systems, known as “molecular Lego”, are of particular interest for their uses in tissue engineering and as biomimetic coatings for medical devices because they can form insoluble macroscopic membranes under physiological conditions. Spectra were collected for both native and gamma-irradiated samples. Quantum mechanical data on two of the examined oligopeptides were also obtained to clarify the assignment of the prominent significative bands observed in the spectra. In general, the peptide–nanoparticles interaction occurs through the COO− groups, with the amide bond and the aliphatic chain close to the colloid surface. After gamma irradiation, mimicking a free oxidative radical attack, the SERS spectra of the biomaterials show that COO− groups still provide the main peptide–nanoparticle interactions. However, the spatial arrangement of the peptides is different, exhibiting a systematic decrease in the distance between aliphatic chains and colloid nanoparticles. Full article
(This article belongs to the Special Issue Peptides and Proteins as Innovative Biomaterials)
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11 pages, 284 KiB  
Article
Characterization and Safety Profile of Transfer Factors Peptides, a Nutritional Supplement for Immune System Regulation
by Hudson Polonini, Any Elisa de Souza Schmidt Gonçalves, Eli Dijkers and Anderson de Oliveira Ferreira
Biomolecules 2021, 11(5), 665; https://doi.org/10.3390/biom11050665 - 29 Apr 2021
Cited by 3 | Viewed by 2196
Abstract
Imuno TF® is a nutritional supplement composed of isolated transfer factors (TF) from porcine spleen. It is composed of a specific mixture of molecules that impact functions of the biological systems and historically is linked to the immune system regulation. In this [...] Read more.
Imuno TF® is a nutritional supplement composed of isolated transfer factors (TF) from porcine spleen. It is composed of a specific mixture of molecules that impact functions of the biological systems and historically is linked to the immune system regulation. In this study, we demonstrate for the first time its proteomic analysis, nutritional composition, and safety profile in terms of mutagenic potential and acute oral dose (LD50). The obtained analysis indicated the product is a complex set of oligo- and polypeptides constituted of 163 different peptides which can potentially act on multiple mechanisms on the immune system pathways. The chemical composition showed low fat and low sugar content, saturated fatty acids-free, and the presence of 10 vitamins and 11 minerals. No mutagenic effect was observed, and the LD50 was 5000 mg kg−1 body weight. This accounts for a safe product to be used by the oral route, with potential benefits for the immune system. Full article
(This article belongs to the Special Issue Peptides and Proteins as Innovative Biomaterials)
17 pages, 2363 KiB  
Article
Mechanistic Insight into Royal Protein Inhibiting the Gram-Positive Bacteria
by Mao Feng, Yu Fang, Chuan Ma, Xiangyuan Duan, Yanyan Zhang, Bin Han, Han Hu, Lifeng Meng, Fuyi Wang and Jianke Li
Biomolecules 2021, 11(1), 64; https://doi.org/10.3390/biom11010064 - 6 Jan 2021
Cited by 8 | Viewed by 2600
Abstract
Royal jelly (RJ), a natural honeybee product, has a wide range of antibacterial activities. N-glycosylated major royal jelly protein 2 (N-MRJP2), purified from RJ, can inhibit the growth of Paenibacillus larvae (P. larvae, Gram-positive), a contagious etiological agent of the American [...] Read more.
Royal jelly (RJ), a natural honeybee product, has a wide range of antibacterial activities. N-glycosylated major royal jelly protein 2 (N-MRJP2), purified from RJ, can inhibit the growth of Paenibacillus larvae (P. larvae, Gram-positive), a contagious etiological agent of the American foulbrood disease of honeybees. However, the inhibitory mechanism is largely unknown. Antibacterial assay and membrane proteome were conducted to investigate the inhibition capacity of RJ from different instar larvae and P. larvae treated by N-MRJP2, respectively. The similar antibacterial efficiency of RJ from different larval instar indicates that RJ is vital for the adaptive immune defense of small larvae. The killing of P. larvae by N-MRJP2 is achieved by disturbing the cell wall biosynthesis, increasing the permeability of cell membrane, hindering aerobic respiration, restraining cell division and inducing cell death. This demonstrates that RJ is critical for the passive immunity of immature larvae and N-MRJP2 can be used as natural antibiotic substance to resist P. larvae, even for other gram-positive bacteria. This constitutes solid evidence that RJ and N-MRJP2 have potentials as novel antibacterial agents. Full article
(This article belongs to the Special Issue Peptides and Proteins as Innovative Biomaterials)
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