» Articles » PMID: 33482828

Sericin Based Nanoformulations: a Comprehensive Review on Molecular Mechanisms of Interaction with Organisms to Biological Applications

Abstract

Background: The advances in products based on nanotechnology have directed extensive research on low-cost, biologically compatible, and easily degradable materials.

Main Body: Sericin (SER) is a protein mainly composed of glycine, serine, aspartic acid, and threonine amino acids removed from the silkworm cocoon (particularly Bombyx mori and other species). SER is a biocompatible material with economic viability, which can be easily functionalized due to its potential crosslink reactions. Also, SER has inherent biological properties, which makes possible its use as a component of pharmaceutical formulations with several biomedical applications, such as anti-tumor, antimicrobials, antioxidants and as scaffolds for tissue repair as well as participating in molecular mechanisms attributed to the regulation of transcription factors, reduction of inflammatory signaling molecules, stimulation of apoptosis, migration, and proliferation of mesenchymal cells.

Conclusion: In this review, the recent innovations on SER-based nano-medicines (nanoparticles, micelles, films, hydrogels, and their hybrid systems) and their contributions for non-conventional therapies are discussed considering different molecular mechanisms for promoting their therapeutic applications.

Citing Articles

Innovative Processing and Sterilization Techniques to Unlock the Potential of Silk Sericin for Biomedical Applications.

Veiga A, Ramirez-Jimenez R, Santos-Rosales V, Garcia-Gonzalez C, Aguilar M, Rojo L Gels. 2025; 11(2).

PMID: 39996657 PMC: 11854797. DOI: 10.3390/gels11020114.


Evaluation of Sericin/Polyvinyl Alcohol Mixtures for Developing Porous and Stable Structures.

Arango M, Vasquez Vasquez L, Parra A, Rueda-Mira S, Jaramillo-Quiceno N, Cerisuelo J Biomimetics (Basel). 2025; 10(1).

PMID: 39851744 PMC: 11762549. DOI: 10.3390/biomimetics10010027.


Synthesis and characterization of selenium nanoparticles stabilized with oxyethylated alkylphenol (neonol) for potential modification of fabric materials.

Rekhman Z, Blinov A, Gvozdenko A, Golik A, Nagdalian A, Blinova A PLoS One. 2024; 19(11):e0314208.

PMID: 39591417 PMC: 11593756. DOI: 10.1371/journal.pone.0314208.


Sericin Protein: Structure, Properties, and Applications.

Aad R, Dragojlov I, Vesentini S J Funct Biomater. 2024; 15(11).

PMID: 39590526 PMC: 11595228. DOI: 10.3390/jfb15110322.


Repurposing of sericin combined with dactolisib or vitamin D to combat non-small lung cancer cells through computational and biological investigations.

Helmy M, Youssef M, Yamari I, Amr A, Moussa F, El Wakil A Sci Rep. 2024; 14(1):27034.

PMID: 39505930 PMC: 11541877. DOI: 10.1038/s41598-024-76947-0.


References
1.
Guo W, Deng L, Chen Z, Chen Z, Yu J, Liu H . Vitamin B12-conjugated sericin micelles for targeting CD320-overexpressed gastric cancer and reversing drug resistance. Nanomedicine (Lond). 2018; 14(3):353-370. DOI: 10.2217/nnm-2018-0321. View

2.
Wang F, Wang Y, Tian C, Xu S, Wang R, Hou K . Fabrication of the FGF1-functionalized sericin hydrogels with cell proliferation activity for biomedical application using genetically engineered Bombyx mori (B. mori) silk. Acta Biomater. 2018; 79:239-252. DOI: 10.1016/j.actbio.2018.08.031. View

3.
Dong Y, Hong M, Dai R, Wu H, Zhu P . Engineered bioactive nanoparticles incorporated biofunctionalized ECM/silk proteins based cardiac patches combined with MSCs for the repair of myocardial infarction: In vitro and in vivo evaluations. Sci Total Environ. 2019; 707:135976. DOI: 10.1016/j.scitotenv.2019.135976. View

4.
Qi Y, Wang H, Wei K, Yang Y, Zheng R, Kim I . A Review of Structure Construction of Silk Fibroin Biomaterials from Single Structures to Multi-Level Structures. Int J Mol Sci. 2017; 18(3). PMC: 5372488. DOI: 10.3390/ijms18030237. View

5.
Zhang Y . Applications of natural silk protein sericin in biomaterials. Biotechnol Adv. 2003; 20(2):91-100. DOI: 10.1016/s0734-9750(02)00003-4. View