Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

13.3K
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...
13.3K
Fibrous Proteins00:55

Fibrous Proteins

3.4K
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
3.4K
Protein and Protein Structure02:15

Protein and Protein Structure

81.4K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
81.4K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.5K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Aptamer-Based Delivery Systems for VEGF and NGF Modulation in Ocular Therapies.

Advanced healthcare materials·2026
Same author

Phosphate- and pH-dependent self-assembly of recombinant spider silk proteins.

Protein science : a publication of the Protein Society·2026
Same author

Biocompatibility of Hydrogels for Glomerular 3D Co-Culture: A Comparative Analysis.

Macromolecular bioscience·2026
Same author

Biofabrication of Endothelialized, Intrinsically Vascularized 3D-Printed Recombinant Spider Silk Scaffolds.

Advanced healthcare materials·2026
Same author

Directed Functionalization of Recombinant Spider Silk Nonwoven Membranes with Antibodies Using Non-Canonical Amino Acids.

Advanced materials (Deerfield Beach, Fla.)·2026
Same author

Convergence of Organ-on-a-Chip and Freeform Printing of Sacrificial Poly(2-cyclopropyl-2-oxazoline) Enables the Generation of Perfusable Endothelialized Channels in Hydrogels.

Macromolecular rapid communications·2026

Related Experiment Video

Updated: Sep 13, 2025

Author Spotlight: Enhancing In Vitro Cell Culture Models with Recombinant Functionalized Spider Silk Membranes
06:17

Author Spotlight: Enhancing In Vitro Cell Culture Models with Recombinant Functionalized Spider Silk Membranes

Published on: November 1, 2024

1.2K

Nanostructured Protein Surfaces Inspired by Spider Silk.

Martin Humenik1, Thomas Scheibel1,2,3,4,5

  • 1Department of Biomaterials, University of Bayreuth, Prof.-Rüdiger-Bormann-Str. 1, 95447, Bayreuth, Germany.

Advanced Materials (Deerfield Beach, Fla.)
|July 29, 2025
PubMed
Summary
This summary is machine-generated.

Recombinant spidroins, inspired by spider silk, are engineered for advanced biomaterials. These protein variants enable precise control over nanostructured surfaces for applications like drug delivery and cell immobilization.

Keywords:
coatingsfunctional materialshydrogelsparticlesself‐assemblyspinning

More Related Videos

Synthetic Spider Silk Production on a Laboratory Scale
13:36

Synthetic Spider Silk Production on a Laboratory Scale

Published on: July 18, 2012

26.9K
Air Filter Devices Including Nonwoven Meshes of Electrospun Recombinant Spider Silk Proteins
09:51

Air Filter Devices Including Nonwoven Meshes of Electrospun Recombinant Spider Silk Proteins

Published on: May 8, 2013

16.3K

Related Experiment Videos

Last Updated: Sep 13, 2025

Author Spotlight: Enhancing In Vitro Cell Culture Models with Recombinant Functionalized Spider Silk Membranes
06:17

Author Spotlight: Enhancing In Vitro Cell Culture Models with Recombinant Functionalized Spider Silk Membranes

Published on: November 1, 2024

1.2K
Synthetic Spider Silk Production on a Laboratory Scale
13:36

Synthetic Spider Silk Production on a Laboratory Scale

Published on: July 18, 2012

26.9K
Air Filter Devices Including Nonwoven Meshes of Electrospun Recombinant Spider Silk Proteins
09:51

Air Filter Devices Including Nonwoven Meshes of Electrospun Recombinant Spider Silk Proteins

Published on: May 8, 2013

16.3K

Area of Science:

  • Biomaterials Science
  • Protein Engineering
  • Nanotechnology

Background:

  • Spider silk proteins (spidroins) exhibit remarkable mechanical properties.
  • Recombinant spidroins are biotechnologically produced variants of natural spider silk proteins.
  • Understanding spidroin self-assembly is key to mimicking natural silk fiber formation.

Purpose of the Study:

  • To review the fabrication of functionalized nanostructured surfaces using recombinant spidroins.
  • To explore molecular engineering strategies for tailoring spidroin interfacial properties.
  • To highlight applications in drug delivery, cell accommodation, and bioselective immobilization.

Main Methods:

  • Utilizing recombinant spidroins to create diverse morphologies (particles, films, hydrogels).
  • Functionalizing spidroins with peptide tags for targeted interactions.
  • Combining spidroin coatings with photo- and soft-lithography for micro/nanopatterning.

Main Results:

  • Demonstrated tailoring of interfacial properties through molecular engineering.
  • Achieved specific drug delivery, cell accommodation, and bioselective immobilization via functionalized spidroins.
  • Produced micro- and nanostructured patterns with defined targeting and affinity properties.

Conclusions:

  • Recombinant spidroins offer a versatile platform for creating advanced biomaterials.
  • Engineered spidroin-based nanostructures have significant potential in biomedical applications.
  • Spidroin functionalization and patterning enable precise control over biological interactions.