Biopanning of mouse bone marrow mesenchymal stem cell affinity for cyclic peptides

Wang, Guozong; Man, Zhentao; Zhang, Nianping; Hua, Xin; Li, Yang; Sun, Tiantong

doi:10.3892/mmr.2018.9626

Cited by 8 publications

(11 citation statements)

References 30 publications

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“…CPs have successfully been used to target a wide range of different classes of proteins, including ‘difficult’ PPIs. While beyond the scope of this review, non‐protein biomolecules and more complex systems can also be targeted by CPs (e.g., lipids, cells), [ 92–94 ] demonstrating the power and versatility of CP genetically encoded library technologies.…”

Section: Discussion and Future Perspectivementioning

confidence: 99%

“…Since the first CP phage display was described over 25 years ago, [13] the CP genetically encoded library technologies have transformed the way ligands are generated for protein targets of interest. The plex systems can also be targeted by CPs (e.g., lipids, cells), [92][93][94] demonstrating the power and versatility of CP genetically encoded library technologies.…”

Section: Discussion and Future Perspectivementioning

confidence: 99%

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Structural diversity inde novocyclic peptide ligands from genetically encoded library technologies

et al. 2020

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Cyclic peptides discovered by genetically encoded library technologies have emerged as a class of promising molecules in chemical biology and drug discovery. Here we review the cyclic peptides identified through these techniques reported in the period 2015 to 2019, with a particular focus on the three‐dimensional structures that peptides adopt when binding to their targets. A range of different structures have been revealed through co‐crystal structures, highlighting how versatile and adaptable these molecules are in binding to diverse protein targets, such as enzymes and receptors, or challenging shallow surfaces involved in protein‐protein interfaces. Analysis of the properties of the peptides reported shows some interesting trends, with further insight for those with structural information suggestive that larger peptides are more likely to adopt secondary structure. We highlight examples where co‐crystal structures have informed the key interactions that promote high affinity and selectivity of cyclic peptides against their targets, identified novel inhibitor binding sites, and provided new insights into the biology of their targets. The structure‐guided modifications have also aided the design of cyclic peptides with improved activity and physicochemical properties. These examples highlight the importance of crystallography in future cyclic peptide drug discovery initiatives.

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Section: Discussion and Future Perspectivementioning

confidence: 99%

Section: Discussion and Future Perspectivementioning

confidence: 99%

Structural diversity inde novocyclic peptide ligands from genetically encoded library technologies

et al. 2020

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“…A fibronectin-derived peptide containing three amino acids (arginine, glycine and aspartic acid), which was confirmed to have a high affinity for BMSCs, was used as the positive control and was termed RGD (21). All of the peptides were chemically synthesized using solid-phase peptide synthesis (Scilight Biotechnology, LLC), according to our previous study (41). The molecular weight of the synthesized C7 was determined using matrix-assisted laser desorption/ionization-time of flight mass spectrometry (JBI Scientific, LLC.)…”

Section: Methodsmentioning

confidence: 99%

A specific affinity cyclic peptide enhances the adhesion, expansion and proliferation of rat bone mesenchymal stem cells on β‑tricalcium phosphate scaffolds

et al. 2019

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osteonecrosis of the femoral head (onFH) is a common osteological disease. Treatment of onFH prior to the collapse of the femoral head is critical for increasing therapeutic efficiency. Tissue engineering therapy using bone mesenchymal stem cells (BMSCs) combined with a scaffold is a promising strategy. However, it is currently unclear how to improve the efficiency of BMSC recruitment under such conditions. In the present study, a specific cyclic peptide for Sprague-Dawley rat BMSCs, CTTNPFSLC (known as C7), was used, which was identified via phage display technology. Its high affinity for BMSCs was demonstrated using flow cytometry and fluorescence staining. Subsequently, the cyclic peptide was placed on β-tricalcium phosphate (β-TcP) scaffolds using absorption and freeze-drying processes. Adhesion, expansion and proliferation of BMSCs was investigated in vitro on the c7-treated β-TcP scaffolds and compared with pure β-TCP scaffolds. The results revealed that C7 had a promoting effect on the adhesion, expansion and proliferation of BMSCs on β-TCP scaffolds. Therefore, C7 may be effective in future tissue engineering therapy for ONFH.

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“…Simply, one could use the peptide to recruit a stem cell population to a biomaterial containing known differentiation cues. This has been demonstrated in a number of studies aimed at identifying peptides specific to marrow stromal cells, with the ultimate goal to functionalize bone-promoting biomaterials for the recruitment of MSCs [ 36 , 37 , 38 , 39 , 40 ]. Alternatively, one could explore if and how the interaction of that peptide with the stem cell population impacts differentiation.…”

Section: Phage Display and Biomaterialsmentioning

confidence: 99%

Phage Display to Augment Biomaterial Function

Davidson

McGoldrick

Kohn

2020

IJMS

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Biomaterial design relies on controlling interactions between materials and their biological environments to modulate the functions of proteins, cells, and tissues. Phage display is a powerful tool that can be used to discover peptide sequences with high affinity for a desired target. When incorporated into biomaterial design, peptides identified via phage display can functionalize material surfaces to control the interaction between a biomaterial and its local microenvironment. A targeting peptide has high specificity for a given target, allowing for homing a specific protein, cell, tissue, or other material to a biomaterial. A functional peptide has an affinity for a given protein, cell, or tissue, but also modulates its target’s activity upon binding. Biomaterials can be further enhanced using a combination of targeting and/or functional peptides to create dual-functional peptides for bridging two targets or modulating the behavior of a specific protein or cell. This review will examine current and future applications of phage display for the augmentation of biomaterials.

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Biopanning of mouse bone marrow mesenchymal stem cell affinity for cyclic peptides

Cited by 8 publications

References 30 publications

Structural diversity inde novocyclic peptide ligands from genetically encoded library technologies

Structural diversity inde novocyclic peptide ligands from genetically encoded library technologies

A specific affinity cyclic peptide enhances the adhesion, expansion and proliferation of rat bone mesenchymal stem cells on β‑tricalcium phosphate scaffolds

Phage Display to Augment Biomaterial Function

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