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Engineered Peptides: Current Applications and Future Perspectives

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 30 July 2024 | Viewed by 3051

Special Issue Editor


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Guest Editor
1. Department of Mechanical Engineering, University of Kansas, 1530 W 15th St Learned Hall Lawrence, Lawrence, KS 66045, USA
2. Institute for Bioengineering Research, University of Kansas, 1530 W 15th St Learned Hall Lawrence, Lawrence, KS 66045, USA
Interests: bio-nano interfaces; bio-nanotechnology; surfaces; biomaterials; tissue engineering; nano-biosensors; biocatalysis molecular biomimetics; bioengineering
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Special Issue Information

Dear Colleagues,

Engineered peptides represent the functional frontiers for the lessons to learn from biological systems to adapt and design functions inspired by proteins. Essentially all fundamental biological processes, including catalysis, metabolism, energy storage, regulation, transport, repair, and maintenance, require proteins that perform diverse functions. Proteins orchestrate cellular and molecular communications, carry out enzymatic reactions, perform regulatory, transport, motor, protective, and structural functions, and control the formation of soft and hard tissues. Peptides designed and engineered to include fundamental molecular information could be an indispensable molecular tool to achieve functional engineering outcomes that are applicable to emerging technologies, including bio-economies, medical, and technological applications.

This Special Issue focuses on the novel design approaches of engineered peptides, their current applications, and emerging functionalities across diverse fields. Peptide and peptide hybrid molecular systems can be engineered to have structural diversity, dynamic and spatial features that exhibit novel functions, unique hierarchical morphologies, and temporal phases. They can be an integral component of functional materials and devices and control bio-hybrid interface interactions.

This Topic welcomes but is not limited to original research, reviews, and mini reviews in the following research areas:

  • Advanced nano-supramolecular technologies;
  • AI/ML methodologies and computational approaches in peptide design, characterization, and targeted functionality;
  • Bioactive, biomimetic peptide design and applications;
  • Engineered peptides in food, agriculture, and bioeconomy;
  • Functional peptide–polymer hybrid interfaces and surfaces;
  • Peptide nanoassemblies;
  • Therapeutic peptides;
  • Peptide drug delivery systems;
  • Peptide-based array and devices structures;
  • Integration of biochemical and chemical diversity into peptide design;
  • Smart biofunctional materials;
  • Peptides at the interface of synthetic biology and materials science.

Prof. Dr. Candan Tamerler
Guest Editor

Manuscript Submission Information

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Keywords

  • AI/ML approaches in peptide design
  • bioactivity biobased bio-nanoassemblies
  • diagnostics drug delivery
  • engineered living materials
  • molecular biomimetics
  • peptides
  • polypeptides self-assembly
  • smart biohybrid materials
  • supramolecular technologies
  • therapeutics

Published Papers (2 papers)

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Research

19 pages, 2398 KiB  
Article
Bioinformatic Approach of B and T Cell Epitopes of PLD and CP40 Proteins of Corynebacterium pseudotuberculosis ovis Mexican Isolate 2J-L towards a Peptide-Based Vaccine
by Maria Carla Rodríguez-Domínguez, Roberto Montes-de-Oca-Jiménez, Juan Carlos Vázquez-Chagoyán, Pilar Eliana Rivadeneira-Barreiro, Pablo Cleomenes Zambrano-Rodríguez, Martha Elba Ruiz-Riva-Palacio, Adriana del Carmen Gutiérrez-Castillo, Siomar de-Castro-Soares, Patricia Vieyra-Reyes and Gabriel Arteaga-Troncoso
Int. J. Mol. Sci. 2024, 25(1), 270; https://doi.org/10.3390/ijms25010270 - 23 Dec 2023
Viewed by 820
Abstract
Mapping B and T cell epitopes constitutes an important action for peptide vaccine design. PLD and CP40 virulence factors of Corynebacterium pseudotuberculosis biovar ovis, a causal agent of Caseous Lymphadenitis, have been evaluated in a murine model as good candidates for vaccine [...] Read more.
Mapping B and T cell epitopes constitutes an important action for peptide vaccine design. PLD and CP40 virulence factors of Corynebacterium pseudotuberculosis biovar ovis, a causal agent of Caseous Lymphadenitis, have been evaluated in a murine model as good candidates for vaccine development. Therefore, the goal of this work was to in silico analyze B and T cell epitopes of the PLD and CP40 proteins of a Mexican isolate of Corynebacterium pseudotuberculosis ovis. The Immune Epitope Data Base and Resource website was employed to predict the linear and conformational B-cell, T CD4+, and T CD8+ epitopes of PLD and CP40 proteins of Corynebacterium pseudotuberculosis ovis Mexican strain 2J-L. Fifty B cell epitopes for PLD 2J-L and forty-seven for CP40 2J-L were estimated. In addition, T CD4+ and CD8+ cell epitopes were predicted for PLD 2J-L (MHC I:16 epitopes, MHC II:10 epitopes) and CP40 2J-L (MHC I: 15 epitopes, MHC II: 13 epitopes). This study provides epitopes, paying particular attention to sequences selected by different predictor programs and overlap sequences as B and T cell epitopes. PLD 2J-L and CP40 2J-L protein epitopes may aid in the design of a promising peptide-based vaccine against Caseous Lymphadenitis in Mexico. Full article
(This article belongs to the Special Issue Engineered Peptides: Current Applications and Future Perspectives)
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23 pages, 9165 KiB  
Article
Engineered Peptides Enable Biomimetic Route for Collagen Intrafibrillar Mineralization
by Aya K. Cloyd, Kyle Boone, Qiang Ye, Malcolm L. Snead, Paulette Spencer and Candan Tamerler
Int. J. Mol. Sci. 2023, 24(7), 6355; https://doi.org/10.3390/ijms24076355 - 28 Mar 2023
Cited by 2 | Viewed by 1898
Abstract
Overcoming the short lifespan of current dental adhesives remains a significant clinical need. Adhesives rely on formation of the hybrid layer to adhere to dentin and penetrate within collagen fibrils. However, the ability of adhesives to achieve complete enclosure of demineralized collagen fibrils [...] Read more.
Overcoming the short lifespan of current dental adhesives remains a significant clinical need. Adhesives rely on formation of the hybrid layer to adhere to dentin and penetrate within collagen fibrils. However, the ability of adhesives to achieve complete enclosure of demineralized collagen fibrils is recognized as currently unattainable. We developed a peptide-based approach enabling collagen intrafibrillar mineralization and tested our hypothesis on a type-I collagen-based platform. Peptide design incorporated collagen-binding and remineralization-mediating properties using the domain structure conservation approach. The structural changes from representative members of different peptide clusters were generated for each functional domain. Common signatures associated with secondary structure features and the related changes in the functional domain were investigated by attenuated total reflectance Fourier-transform infrared (ATR-FTIR) and circular dichroism (CD) spectroscopy, respectively. Assembly and remineralization properties of the peptides on the collagen platforms were studied using atomic force microscopy (AFM). Mechanical properties of the collagen fibrils remineralized by the peptide assemblies was studied using PeakForce-Quantitative Nanomechanics (PF-QNM)-AFM. The engineered peptide was demonstrated to offer a promising route for collagen intrafibrillar remineralization. This approach offers a collagen platform to develop multifunctional strategies that combine different bioactive peptides, polymerizable peptide monomers, and adhesive formulations as steps towards improving the long-term prospects of composite resins. Full article
(This article belongs to the Special Issue Engineered Peptides: Current Applications and Future Perspectives)
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