Ecm-mimetic Peptides
Ecm-mimetic Peptides - Related Videos
07:03
Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Cited by 18 •
2014
This procedure demonstrates in vivo near IR fluorescence imaging of collagen remodeling activities in mice as well as ex vivo staining of collagens in tissue sections using caged collagen mimetic peptides that can be photo-triggered to hybridize with denatured collagen strands.
09:39
Targeted Antibody Blocking by a Dual-Functional Conjugate of Antigenic Peptide and Fc-III Mimetics (DCAF)
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2019
Development of a dual-functional conjugate of antigenic peptide and Fc-III mimetics (DCAF) is novel for the elimination of harmful antibodies. Here, we describe a detailed protocol for the synthesis of DCAF1 molecule, which can selectively block 4G2 antibody to eliminate antibody dependent enhancement effect during Dengue virus infection.
16:33
ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
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Cited by 17 •
2014
A method to obtain nanofibers and complex nanostructures from single or multiple extracellular matrix proteins is described. This method uses protein-surface interactions to create free-standing protein-based materials with tunable composition and architecture for use in a variety of tissue engineering and biotechnology applications.
04:16
ECM Suspension Preparation: A Technique to Obtain Homogenous Suspension from Tissue-derived Extracellular Matrix
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2023
This video describes the preparation of a homogenized and digested extracellular matrix suspension from decellularized and lyophilized tissues. This technique helps in fabricating ECM-derived porous foams and microcarriers for use as substrates in advanced 3D cell culture models.
01:25
Fibronectins Connect Cells with ECM
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2023
Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal. Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
FAQs
Their binding motifs provide recognizable signals that interact with cell receptors, influencing how cells respond to a surrounding material. Depending on the cues presented, these interactions can support cell adhesion, migration, or tissue organization. This receptor-level control allows bioengineers to connect a peptide’s sequence design with specific cellular responses in engineered microenvironments.
Reproducing selected cues gives researchers greater control over which biological signals a material presents. Instead of recreating every feature of the extracellular matrix, they can focus on signals relevant to a particular experimental or therapeutic goal. This selective approach supports deliberate tuning of biological activity while maintaining control over the material’s composition.
The amino-acid sequence determines which matrix-like signals or binding motifs the material can present to cells. Incorporating sequences with different biological activities can therefore alter the signals available within a scaffold, hydrogel, or related material. This design flexibility helps researchers create microenvironments tailored to cellular adhesion, migration, tissue organization, or other selected outcomes.
These peptides can be incorporated into hydrogels, scaffolds, and other biomaterials so that the resulting material presents controlled matrix-like cues to cells. The surrounding material provides the engineered environment, while the peptide contributes selected biochemical or structural signals. This combination connects material composition with biological activity in a format suitable for controlled cellular studies.
Selection depends on the cellular response and experimental or therapeutic objective the material must support. Researchers can choose peptide sequences according to the matrix-like signals they want to present, then incorporate them into a compatible biomaterial format. This goal-directed design helps align peptide activity, material composition, and the intended cellular microenvironment.
In bioengineering, these peptides support cell-compatible materials for tissue engineering, wound repair, drug delivery, and in vitro models. Their value lies in providing controllable biological activity within engineered materials, allowing researchers to study or influence cellular behavior in defined environments. The same design principle can therefore serve both experimental model development and therapeutic material design.