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Recent Advances in Peptide Assembly and Bioactivity

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: 31 December 2025 | Viewed by 172

Special Issue Editor


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Guest Editor
College of Chemistry, Jilin University, Changchun, China
Interests: peptide assembly; polycondensate; underwater adhesive; antimicrobial; tissue sealant
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Peptide self-assembly has emerged as a transformative strategy in engineering bioactive materials, offering unparalleled advantages in biocompatibility and therapeutic precision. A growing body of evidence has elucidated its critical role in modulating fundamental biological processes, ranging from gene delivery and transcriptional regulation to antimicrobial interventions and growth factor stabilization. These supramolecular architectures demonstrate remarkable pharmacokinetic enhancements, including extended systemic circulation, optimized cellular uptake kinetics, and spatiotemporal targeting specificity. Particularly noteworthy is their inherent dynamic adaptability, which confers stimuli-responsive reconfiguration capabilities. This unique property enables the development of intelligent material platforms with programmable bioactivity modulation, creating unprecedented opportunities for precision biomedical applications.

We are pleased to invite you to contribute groundbreaking original research or state-of-the-art reviews to this Special Issue on "Recent Advances in Peptide Assembly and Bioactivity". This collection will highlight innovative self-assembling peptide systems and hybrid co-assemblies that address pressing biomedical challenges, with a particular emphasis on elucidating structure-bioactivity relationships. Submissions exploring novel assembly mechanisms, advanced characterization methodologies, or translational applications across therapeutic domains are especially encouraged.

Prof. Dr. Wen Li
Guest Editor

Manuscript Submission Information

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Keywords

  • peptide
  • self-assembly
  • co-assembly
  • stimuli-responsive
  • bioactivity
  • biomaterials

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Published Papers (1 paper)

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Research

15 pages, 3697 KB  
Article
Virus-like Particles Formed by the Coat Protein of the Single-Stranded RNA Phage PQ465 as a Carrier for Antigen Presentation
by Egor A. Vasyagin, Eugenia S. Mardanova and Nikolai V. Ravin
Molecules 2025, 30(20), 4056; https://doi.org/10.3390/molecules30204056 (registering DOI) - 11 Oct 2025
Abstract
Virus-like particles (VLPs) formed as a result of self-assembly of viral capsid proteins are widely used as a platform for antigen presentation in vaccine development. However, since the inclusion of a foreign peptide into the capsid protein can alter its spatial structure and [...] Read more.
Virus-like particles (VLPs) formed as a result of self-assembly of viral capsid proteins are widely used as a platform for antigen presentation in vaccine development. However, since the inclusion of a foreign peptide into the capsid protein can alter its spatial structure and interfere with VLP assembly, such insertions are usually limited to short peptides. In this study, we have demonstrated the potential of capsid protein (CP) of single-stranded RNA phage PQ465 to present long peptides using green fluorescent protein (GFP) as a model. GFP was genetically linked to either the N- or C-terminus of PQ465 CP. Hybrid proteins were expressed in Escherichia coli and Nicotiana benthamiana plants. Spherical virus-like particles (~35 nm according to transmission electron microscopy) were successfully formed by both N- and C-terminal fusions expressed in E. coli, and by plant-produced CP with GFP fused to the C-terminus. ELISA revealed that GFP in VLPs was accessible for specific antibodies suggesting that it is exposed on the surface of PQ465-GFP particles. VLPs carrying GFP were recognized by anti-CP antibodies with less efficiency than VLPs formed by empty CP, which indicates shielding of the CP core in PQ465-GFP particles. Therefore, PQ465 CP can be used as a chimeric VLP platform for the display of relatively large protein antigens, which can operate in bacterial and plant expression systems. Full article
(This article belongs to the Special Issue Recent Advances in Peptide Assembly and Bioactivity)
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