Self-Assembled Peptides Advanced Platform for Modern Drug Delivery
Self-Assembled Peptides: Advanced Platform for Modern Drug Delivery
1.Research Background
Peptide-based biomaterials have drawn widespread attention in the biomedical field for their excellent biocompatibility, biodegradability and design flexibility. Self-assembled peptides can spontaneously form ordered nanostructures including nanospheres, nanofibers and hydrogels via hydrogen bonding, hydrophobic interaction, electrostatic force and other non-covalent forces. Traditional drugs often suffer from poor water solubility, non-specific distribution, short in-vivo half-life and easy degradation after administration. As a novel delivery carrier, self-assembled peptide nanostructures can effectively solve these pain points, and gradually become a research hotspot for the delivery of small-molecule drugs, nucleic acid drugs, polypeptide and protein therapeutics.
2.Research Purpose and Significance
This work systematically summarizes the structural characteristics, assembly rules, biocompatibility and stability of self-assembled peptides, and sorts out their application effects in delivering three major categories of drugs. It analyzes the advantages and existing limitations of different peptide delivery systems in actual scenarios. The research provides clear theoretical support and practical reference for the development, optimization and industrial transformation of peptide-based drug delivery carriers, and lays a foundation for developing high-efficiency, low-toxicity targeted delivery solutions for clinical drugs.
3.Research Content
The self-assembly behavior of peptides is jointly determined by amino acid sequences, secondary structures and external conditions such as pH, temperature and ion concentration. These peptide materials feature low immunogenicity, good degradability and controllable stability, and can achieve dynamic balance between structural stability and on-demand disassembly in physiological environments.
In practical application, self-assembled peptide carriers show distinct performance for different drugs. For small-molecule drugs such as antitumor and antibacterial agents, peptides can encapsulate active ingredients to improve solubility and tissue targeting, realizing local controlled release. For nucleic acid drugs like siRNA and DNA, cationic peptide assemblies can protect nucleic acids from enzymatic degradation and boost intracellular delivery efficiency. For polypeptide and protein drugs including GLP-1 analogs, peptide hydrogels and nanofiber reservoirs can extend circulation time, achieve sustained release and reduce administration frequency.
At present, the application still faces challenges: the predictability of peptide assembly needs to be improved, and the stability of nanostructures in complex in-vivo environments requires further enhancement. Meanwhile, problems such as inconsistent batch performance and difficulties in large-scale production also restrict further clinical promotion.
4.Conclusion & Outlook
Self-assembled peptides have proven to be versatile and high-performance drug delivery platforms, capable of adapting to the delivery demands of multiple drug types and delivering targeted, sustained and controlled release effects; looking ahead, the industry will focus on developing smart stimuli-responsive peptides that respond to pH, enzyme and redox signals, and explore combined systems integrated with liposomes, polymer nanoparticles and cell-penetrating peptides to achieve synergistic advantages. In addition, researchers will further optimize peptide sequence design, standardize production processes, enhance batch stability and large-scale preparation capacity, and accelerate the clinical translation of self-assembled peptide delivery systems, so as to create more safe and efficient delivery solutions for precision therapy.
Reference: Wu Hao, Lü Huawei, Li Xingnuo. Recent Advances in the Application of Self-Assembling Peptides in Drug Delivery [J/OL]. Pharmacy Today, 1–14 [17 June 2026]. https://link.cnki.net/urlid/44.1650.R.20260509.1027.004.
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