Related Experiment Video

Updated: Jan 24, 2026

Author Spotlight: Innovative Microneedle-Based Strategies for Enhanced Exosome Delivery and Stability
07:41

Author Spotlight: Innovative Microneedle-Based Strategies for Enhanced Exosome Delivery and Stability

Published on: July 12, 2024

3.5K

Protein-Capturing Microgel-Integrated Microneedle Array Patches for Enhanced Tip-Loading, Storage Stability, and

Ki Hyun Bae1, Kun Liang2,3, Brandon Y L Seow1

  • 1Bioprocessing Technology Institute (BTI), Agency for Science, Technology and Research (A*STAR), Singapore, Republic of Singapore.

Small (Weinheim an Der Bergstrasse, Germany)
|January 23, 2026
PubMed

Keywords:
SARS‐CoV‐2microgelsmicroneedlestransdermalvaccines

More Related Videos

Polymeric Microneedle Array Fabrication by Photolithography08:15

Polymeric Microneedle Array Fabrication by Photolithography

Published on: November 17, 2015

12.9K
Evaluation of the Storage Stability of Extracellular Vesicles11:31

Evaluation of the Storage Stability of Extracellular Vesicles

Published on: May 22, 2019

15.0K

Related Concept Videos

Bioavailability Enhancement: Drug Stability Enhancement and GI Retention01:05

Bioavailability Enhancement: Drug Stability Enhancement and GI Retention

Body:Improving a drug's stability in the gastrointestinal (GI) tract is paramount for enhancing its bioavailability and therapeutic effectiveness. Various strategies are employed to protect the drug from the harsh gastric milieu and to ensure its release and absorption at the desired site within the GI tract.Polymer coatings are one such method used to shield drugs from the stomach's acidic environment. By preventing premature drug release, these coatings improve the bioavailability of unstable...
203
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.1K
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
19.7K
Homologous Recombination02:31

Homologous Recombination

The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
62.8K
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.6K