Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

TGF - β Signaling Pathway

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...

You might also read

Related Articles

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

Sort by

Same author

Advanced biomaterial strategies for 3D <i>in vitro</i> biomimetic neuroblastoma cell culture.

Biomaterials science·2026

Same author

Reshaping the glycocalyx: the SULF extracellular endosulfatases as molecular editors of heparan Sulfate.

The Biochemical journal·2026

Same author

CCHFV GP38 and GP85 interact with cell-surface glycosaminoglycans.

Npj viruses·2026

Same author

Human Sulfatases Use Dual Mechanisms to Control Growth Factor-Heparan Sulfate Interactions.

ACS chemical biology·2026

Same author

Proteoglycofili are glycosaminoglycan-containing fibrillar components released by neutrophils to neutralize bacteria.

Cell reports·2025

Same author

Correction to "BMP-Binding Polysulfonate Brushes to Control Growth Factor Presentation and Regulate Matrix Remodelling".

ACS applied materials & interfaces·2025

Search research articles

Related Experiment Video

Updated: Jun 14, 2025

Site-Directed Immobilization of Bone Morphogenetic Protein 2 to Solid Surfaces by Click Chemistry

Site-Directed Immobilization of Bone Morphogenetic Protein 2 to Solid Surfaces by Click Chemistry

Published on: March 29, 2018

BMP2 Binds Non-Specifically to PEG-Passivated Biomaterials and Induces pSMAD 1/5/9 Signalling.

Jean Le Pennec¹, Amaury Guibert¹, Raviteja Gurram^1,2

¹Université Grenoble Alpes, INSERM, CEA, CNRS, U1292 Biosanté, EMR 5000, Grenoble, 38000, France.

Macromolecular Bioscience

|August 31, 2024

Summary

Non-specific binding of bone morphogenetic protein 2 (BMP2) to biomaterials can skew research findings. A blocking strategy using bovine serum albumin and trehalose effectively prevents this issue, improving data reliability.

Keywords:

BMP2 biomaterials non‐specific streptavidin platforms

More Related Videos

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach

Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach

Published on: August 26, 2013

Related Experiment Videos

Last Updated: Jun 14, 2025

Site-Directed Immobilization of Bone Morphogenetic Protein 2 to Solid Surfaces by Click Chemistry

Site-Directed Immobilization of Bone Morphogenetic Protein 2 to Solid Surfaces by Click Chemistry

Published on: March 29, 2018

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach

Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach

Published on: August 26, 2013

Area of Science:

Biomaterials Science
Cellular Signaling
Surface Chemistry

Background:

Biomaterials are crucial for studying cellular responses to extracellular matrix components.
Investigating glycosaminoglycans (GAGs) role in bone morphogenetic protein 2 (BMP2) signaling is vital for regenerative medicine.
Non-specific protein adsorption on biomaterials complicates experimental interpretation.

Purpose of the Study:

To investigate the role of GAGs in BMP2 signaling using streptavidin platforms.
To identify and implement strategies to prevent non-specific BMP2 adsorption on biomaterials.
To validate the effectiveness of blocking strategies on different biomaterial surfaces.

Main Methods:

Development of streptavidin platforms for biomaterial studies.
Assessment of non-specific BMP2 adsorption using anti-fouling polyethylene glycol (PEG) chains.
Screening of blocking agents, identifying a combination of bovine serum albumin and trehalose.
Comparative analysis of blocking efficiency on glass and gold surfaces with Chinese hamster ovary (CHO) cells.

Main Results:

Residual non-specific BMP2 adsorption persisted even with PEG incorporation, triggering signaling.
A blocking condition using bovine serum albumin and trehalose successfully prevented non-specific BMP2 adsorption.
The blocking strategy demonstrated improved efficacy on gold platforms compared to glass.
Enhanced BMP2 signaling was observed with Chinese hamster ovary (CHO) cells.

Conclusions:

Non-specific adsorption of BMP2 on biomaterials is a significant, often undetected, challenge.
Effective blocking strategies are essential for accurate interpretation of cellular responses in biomaterial research.
The identified blocking method offers a reliable approach to mitigate non-specific binding, enhancing biomaterial study validity.
Surface material choice (gold vs. glass) impacts blocking efficiency, highlighting the need for tailored approaches.