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Peptide Self-Assembly
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Peptide Self-Assembly

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

Deadline for manuscript submissions: 20 September 2025 | Viewed by 1090

Special Issue Editor

Dr. Yi Jia

E-Mail Website
Guest Editor
Beijing National Laboratory for Molecular Sciences, CAS Key Lab of Colloid, Interface and Chemical Thermodynamics, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, China
Interests: peptide self-assembly; biomolecular motor; schiff base; layer-by-layer assembly; dopamine; drug delivery; nanomedicine
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Peptides are fundamental molecular building blocks that reflect their pivotal roles as central structural elements of the biological systems. Ordered peptide assemblies at the nano-, micro-, and macroscale enable living organisms to execute their physiological functions, and biology is harnessing the unique physical properties of these assemblies. Peptides exhibit biocompatibility and chemical diversity characteristics akin to those of proteins while also possessing distinctive characteristics such as relatively high stability, structural simplicity, ease of production, and flexibility in molecular design. Peptides and their derivatives can spontaneously assemble into diverse structures with intriguing and tunable physicochemical properties. Applications of peptide materials are therefore rich in variety, encompassing drug delivery systems, tissue regeneration, supercapacitors, and biosensors. Contributions to this Special Issue will present the latest advances as well as new insights into the mechanism and assembly of peptide materials, deepen our understanding of their biological role in life processes, and reveal innovative peptide-based functional materials and emerging applications.

Dr. Yi Jia
Guest Editor

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Keywords

  • peptide assembly
  • aromatic short peptides
  • bioinspired supramolecular architectures
  • functional materials
  • peptide microfabrication
  • anticancer therapy
  • supercapacitor
  • biosensing

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Published Papers (2 papers)

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Research

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16 pages, 4149 KiB  
Article
Hydrophilic Sulfonate Covalent Organic Frameworks for Serum Glycopeptide Profiling
by Shishu Yang, Yuheng Jiang, Shijie Jiang, Lihong Liu, Si Liu, Hua Zhang and Zhiyuan Gu
Int. J. Mol. Sci. 2025, 26(5), 1957; https://doi.org/10.3390/ijms26051957 - 24 Feb 2025
Viewed by 546
Abstract
Aberrant protein glycosylation is closely associated with a number of biological processes and diseases. However, characterizing the types of post-translational modifications (PTMs) from the complex biological samples is challenging for comprehensive glycoproteomic analysis. The development of high-performance enrichment materials and strategies during the [...] Read more.
Aberrant protein glycosylation is closely associated with a number of biological processes and diseases. However, characterizing the types of post-translational modifications (PTMs) from the complex biological samples is challenging for comprehensive glycoproteomic analysis. The development of high-performance enrichment materials and strategies during the sample pretreatment process is a prerequisite to glycoproteome research. Here in this work, a sulfonate-rich covalent organic framework (COF) called TpPa-(SO3H)2 (referred to as SCOF-2) was synthesized using the Schiff base reaction for the identification of glycopeptides. Benefiting from high hydrophilicity and abundant sulfonate affinity, a total of 28 and 16 glycopeptides could be efficiently detected from the standard glycoproteins of horseradish peroxidase (HRP) and immunoglobulin G (IgG) tryptic digest, respectively. Moreover, the as-prepared sulfonate-rich SCOF-2 has an ultralow detection limit (0.01 fmol μL−1), excellent enrichment selectivity (molar ratio HRP:BSA = 1:5000), satisfactory recovery rate (89.1%), high adsorption capacity (150 mg g−1) and good reusability in the individual enrichment. Meanwhile, by using the SCOF-2 adsorbent, 196 and 194 endogenous glycopeptides in the serum of ovarian cancer patients and healthy people among triplicates were successfully enriched and identified, respectively, using combined nanoLC–MS/MS technology. It demonstrated its great application potential in glycoproteomics research and provided a novel insight for the design of affinity materials. Full article
(This article belongs to the Special Issue Peptide Self-Assembly)
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Review

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21 pages, 6154 KiB  
Review
Probing Peptide Assembly and Interaction via High-Resolution Imaging Techniques: A Mini Review
by Xiaoming Zhang, Zhanshu Yang, Jiaxuan Lin, Wei Zhou, Nan Sun and Yi Jia
Int. J. Mol. Sci. 2025, 26(9), 3998; https://doi.org/10.3390/ijms26093998 - 23 Apr 2025
Viewed by 229
Abstract
Peptide molecules, as fundamental structural units in biological systems, play pivotal roles in diverse biological processes and have garnered substantial attention in biomolecular self-assembly research. Their structural simplicity and high design flexibility make peptides key players in the development of novel biomaterials. High-resolution [...] Read more.
Peptide molecules, as fundamental structural units in biological systems, play pivotal roles in diverse biological processes and have garnered substantial attention in biomolecular self-assembly research. Their structural simplicity and high design flexibility make peptides key players in the development of novel biomaterials. High-resolution imaging techniques have provided profound insights into peptide assembly. Recently, the development of cutting-edge technologies, such as super-resolution microscopy (SRM) with unparalleled spatiotemporal resolution, has further advanced peptide assembly research. These advancements enable both the mechanistic exploration of peptide assembly pathways and the rational design of peptide-based functional materials. In this mini review, we systematically examine the structural diversity of peptide assemblies, including micelles, tubes, particles, fibers and hydrogel, as investigated by various high-resolution imaging techniques, with a focus on their assembly characterization and dynamic process. We also summarize the interaction networks of peptide assemblies with proteins, polymers and microbes, providing further insight into the interactions between peptide assemblies and other molecules. Furthermore, we emphasize the transformative role of high-resolution imaging techniques in addressing long-standing challenges in peptide nanotechnology. We anticipate that this review will accelerate the advancement of peptide assembly characterization, thereby fostering the creation of next-generation functional biomaterials. Full article
(This article belongs to the Special Issue Peptide Self-Assembly)
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