Spatial Organization of Functional Groups on Bioactive Supramolecular Glycopeptide Nanofibers for Differentiation of Mesenchymal Stem Cells (MSCs) to Brown Adipogenesis

Çalışkan, Özüm Şehnaz; Ekiz, Melis Sardan; Tekinay, Ayşe B.; Güler, Mustafa O.

doi:10.1021/acs.bioconjchem.6b00632

Cited by 16 publications

(15 citation statements)

References 54 publications

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“…Notably, glycosylation facilitates hierarchical assembly of various natural protein-based structures, including acetylcholine receptors, flagella, and mucinous liquid crystals [20][21][22] . Peptide-based nanofibers modified with carbohydrates are finding increasing use as biomaterials for various applications, including growth factor delivery, lectin recognition, cell binding, and tissue regeneration [23][24][25][26][27][28][29][30] . Yet, the influence of glycosylation on synthetic peptide self-assembly has received only limited attention focused primarily on hydrogel formation, nanofiber morphology, and nanofiber solubility 31,32 .…”

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confidence: 99%

Hierarchical self-assembly and emergent function of densely glycosylated peptide nanofibers

et al. 2019

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Glycosylation alters protein form and function by establishing intermolecular forces that mediate specific interactions while preventing non-specific aggregation. Self-assembled peptide nanofibers modified with carbohydrates are increasingly used as biomaterials to mimic glycosylated protein function, yet the influence of carbohydrate conjugates on nanofiber structure remains poorly defined. Here we show that a dense carbohydrate surface layer can facilitate hierarchical organization of peptide nanofibers into anisotropic networks. Glycosylated peptide nanofibers remain dispersed in dilute conditions, whereas non-glycosylated nanofibers tend to aggregate. In crowded conditions, some glycosylated nanofibers laterally associate and align. This behavior depends on carbohydrate chemistry, particularly hydroxyls, suggesting involvement of short-range attractive forces. Macroscopic gels fabricated from densely glycosylated peptide nanofibers are resistant to non-specific interactions with proteins, mammalian cells, and bacteria, yet selectively bind lectins, analogous to natural lowfouling mucosal barriers. Collectively, these observations demonstrate that glycosylation can inform structure in addition to endowing function to peptide-based supramolecular biomaterials.

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confidence: 99%

Hierarchical self-assembly and emergent function of densely glycosylated peptide nanofibers

et al. 2019

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“…Tekinay and Guler explored the effect of different spatial arrangements of displayed carboxy, amine, and glucose groups on peptide amphiphile (PA) nanofibers on the differentiation of mesenchymal stem cells (MSCs). [115] Four peptide amphiphiles ( An innovative application of multivalent display on assembled peptide scaffolds for regenerative medicine has been recently reported that targets denatured collagen (dColl) by displaying a collagen hybridizing peptide (CHP). [58] Collagen is the most abundant protein in mammals playing crucial roles in cellular activities such as proliferation, differentiation, and regeneration.…”

Section: Other Chemical Signals For Tissue Engineeringmentioning

confidence: 99%

“…Chemical structures of Tekinay and Guler's peptide amphiphiles. [115] Black is the lauryl alkyl tail, blue is the GAVV β-sheet motif, red is Glu, magenta is Lys, and green is Ser(OGlc) F I G U R E 9 A, Chemical structure of a collagen hybridizing peptide (GPO) 9 conjugated to the β-sheet self-assembling (FKFE) 2 peptide. B, Schematic representation of the self-assembled bilayer of (FKFE) 2 presenting the collagen hybridizing peptide in a multivalent array.…”

Section: Vaccines and Immunomodulatory Materialsmentioning

confidence: 99%

Multivalent display of chemical signals on self‐assembled peptide scaffolds

et al. 2021

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Self-assembled peptide materials have emerged as promising bioinspired tools for applications that include regenerative medicine, drug delivery, antimicrobial and vaccine development, optics, and catalysis. Peptide self-assembly mediated by noncovalent hydrogen bonding, coulombic, hydrophobic, and aromatic interactions gives rise to a variety of supramolecular structures that reflect on the nature of the constituent peptides. The emergent properties of these supramolecular peptide materials often depend on the multivalent presentation of functional appendages on the self-assembled scaffold. For example, the multivalent display of cell-signaling motifs on self-assembled peptide nanofibrils provides materials that are excellent extracellular matrix mimetics for tissue engineering applications. This review includes a discussion of chemical strategies that address the challenge of appending functional signal motifs in a multivalent display on self-assembled peptide and protein materials. In addition, recent examples of supramolecular peptide materials that rely on the multivalent display of chemical signals for the desired applications are presented. Collectively, this discussion illustrates the potential of self-assembled peptides as sustainable materials to address challenges in contemporary materials science and provides principles for the design of next-generation agents for a variety of applications.

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“…One emerging application of glycopeptides is to create nanomaterials that can mediate cell adhesion or activate cell signaling events by interacting with carbohydrate-binding receptors [87,88,89]. For example, Guler and co-workers used glycopeptide amphiphiles to fabricate glycosaminoglycan (GAG)-like nanomaterials.…”

Section: Moving Beyond Peptides As the Functional Ligandmentioning

confidence: 99%

“…The same group also created an extracellular matrix (ECM)-mimicking scaffold using glycopeptide amphiphiles, which enhanced MSC adhesion. By altering the presentation of different functional groups, these scaffolds could induce differentiation of MSCs into brown adipocytes [89]. Additionally, they developed a self-assembled mannosylated peptide amphiphile decorated with antigen-mimetic GM3-lactone molecules as the basis for vaccines that target dendritic cells and induce their maturation [87].…”

Section: Moving Beyond Peptides As the Functional Ligandmentioning

confidence: 99%

Using Self-Assembling Peptides to Integrate Biomolecules into Functional Supramolecular Biomaterials

Liu

Hudalla

2019

Molecules

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Throughout nature, self-assembly gives rise to functional supramolecular biomaterials that can perform complex tasks with extraordinary efficiency and specificity. Inspired by these examples, self-assembly is increasingly used to fabricate synthetic supramolecular biomaterials for diverse applications in biomedicine and biotechnology. Peptides are particularly attractive as building blocks for these materials because they are based on naturally derived amino acids that are biocompatible and biodegradable; they can be synthesized using scalable and cost-effective methods, and their sequence can be tailored to encode formation of diverse architectures. To endow synthetic supramolecular biomaterials with functional capabilities, it is now commonplace to conjugate self-assembling building blocks to molecules having a desired functional property, such as selective recognition of a cell surface receptor or soluble protein, antigenicity, or enzymatic activity. This review surveys recent advances in using self-assembling peptides as handles to incorporate biologically active molecules into supramolecular biomaterials. Particular emphasis is placed on examples of functional nanofibers, nanovesicles, and other nano-scale structures that are fabricated by linking self-assembling peptides to proteins and carbohydrates. Collectively, this review highlights the enormous potential of these approaches to create supramolecular biomaterials with sophisticated functional capabilities that can be finely tuned to meet the needs of downstream applications.

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Spatial Organization of Functional Groups on Bioactive Supramolecular Glycopeptide Nanofibers for Differentiation of Mesenchymal Stem Cells (MSCs) to Brown Adipogenesis

Cited by 16 publications

References 54 publications

Hierarchical self-assembly and emergent function of densely glycosylated peptide nanofibers

Hierarchical self-assembly and emergent function of densely glycosylated peptide nanofibers

Multivalent display of chemical signals on self‐assembled peptide scaffolds

Using Self-Assembling Peptides to Integrate Biomolecules into Functional Supramolecular Biomaterials

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