Dynamic peptide libraries for the discovery of supramolecular nanomaterials

Pappas, Charalampos G.; Shafi, Ramim; Sasselli, Ivan R.; Siccardi, Henry; Wang, Tong; Narang, V.; Abzalimov, Rinat R.; Wijerathne, Nadeesha; Ulijn, Rein V.

doi:10.1038/nnano.2016.169

Cited by 197 publications

(201 citation statements)

References 44 publications

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“…Oligopeptides that consist of amino acids with aliphatic side chains have received less attention 21, 22. Furthermore, outside of tripeptide assemblies, there have only been a few studies which focused on oligopeptide sequences that are slightly extended in length (4–8 amino acids).…”

mentioning

confidence: 99%

Tunable Pentapeptide Self‐Assembled β‐Sheet Hydrogels

2018

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Oligopeptide‐based supramolecular hydrogels hold promise in a range of applications. The gelation of these systems is hard to control, with minor alterations in the peptide sequence significantly influencing the self‐assembly process. We explored three pentapeptide sequences with different charge distributions and discovered that they formed robust, pH‐responsive hydrogels. By altering the concentration and charge distribution of the peptide sequence, the stiffness of the hydrogels could be tuned across two orders of magnitude (2–200 kPa). Also, through reassembly of the β‐sheet interactions the hydrogels could self‐heal and they demonstrated shear‐thin behavior. Using spectroscopic and cryo‐imaging techniques, we investigated the relationship between peptide sequence and molecular structure, and how these influence the mechanical properties of the hydrogel. These pentapeptide hydrogels with tunable morphology and mechanical properties have promise in tissue engineering, injectable delivery vectors, and 3D printing applications.

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mentioning

confidence: 99%

Tunable Pentapeptide Self‐Assembled β‐Sheet Hydrogels

2018

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“…Although thermodynamic control of the equilibrium for enzymatic peptide formation can be applied during the synthesis of small peptides or fragment coupling, it is insufficient for polypeptide preparation resulting from sequential steps of aminolysis. [35][36][37] The aminolysis reaction can be kinetically accelerated by using moderately activated acyl donors (generally, amino acid esters). The ester group of amino acid derivatives reacts rapidly with catalytic cysteine or serine to produce an activated intermediate, followed by aminolysis, which creates an amide bond.…”

Section: Mechanismmentioning

confidence: 99%

Chemoenzymatic Synthesis of Polypeptides for Use as Functional and Structural Materials

Tsuchiya

Numata

2017

Macromolecular Bioscience

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Polypeptides inspired by the natural functional and structural proteins present in living systems are promising materials for various fields in terms of their versatile functionality and physical properties. Designing and synthesizing mimetic sequences of specific peptide motifs in proteins are important for exploring the functionality of natural proteins. Chemoenzymatic polymerization, which utilizes aminolysis (i.e., the reverse reaction of hydrolysis catalyzed by proteases), is a useful technique for synthesizing artificial polypeptide materials and has several advantages, including facile synthesis protocols, environmental friendliness, scalability, and atom economy. In this review, recent progress in chemoenzymatic polypeptide synthesis for the production of functional and structural materials for various applications is summarized in conjunction with the current status of technical challenges in the field.

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“…An increasing number of strategies aim to fabricate, through molecular self-assembly, hierarchical structures with precision and tuneability [1,3,[9][10][11][12]. Our group has recently reported a co-assembling system based on the conformational modification of elastin-like recombinamers (ELRs) by peptide amphiphiles (PAs) that enables the fabrication of membranes with the capacity to undergo morphogenesis into complex tubular micro/macro structures [10].…”

Section: U N C O R R E C T E D P R O O Fmentioning

confidence: 99%

“…Four exogenous cross-linkers frequently used in tissue engineering applications [13,[16][17][18]23,30,31] were used including glutaraldehyde (GTA) [16,17,32], genipin (GNP) [15,22,33], poly (ethylene glycol) ether tetrasuccinimidyl glutarate (4S-PEG) [12,17,30,31], and succinimidyl carboxymethyl ester (SCM-PEG-SCM) [29,34] (Fig. 2).…”

Section: Crosslinking Strategiesmentioning

confidence: 99%

Cross-linking of a biopolymer-peptide co-assembling system

et al. 2017

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The ability to guide molecular self-assembly at the nanoscale into complex macroscopic structures could enable the development of functional synthetic materials that exhibit properties of natural tissues such as hierarchy, adaptability, and self-healing. However, the stability and structural integrity of these kinds of materials remains a challenge for many practical applications. We have recently developed a dynamic biopolymer-peptide co-assembly system with the capacity to grow and undergo morphogenesis into complex shapes. Here we explored the potential of different synthetic (succinimidyl carboxymethyl ester [SCM-PEG-SCM], poly (ethylene glycol) ether tetrasuccinimidyl glutarate [4S-StarPEG] and glutaraldehyde) and natural (genipin) cross-linking agents to stabilize membranes made from these biopolymer-peptide co-assemblies. We investigated the cross-linking efficiency, resistance to enzymatic degradation, and mechanical properties of the different cross-linked membranes. We also compared their biocompatibility by assessing the metabolic activity and morphology of adipose-derived stem cells (ADSC) cultured on the different membranes. While all cross-linkers successfully stabilized the system under physiological conditions, membranes cross-linked with genipin exhibited better resistance in physiological environments, improved stability under enzymatic degradation, and a higher degree of in vitro cytocompatibility compared to the other cross-linking agents. The results demonstrated that genipin is an attractive candidate to provide functional structural stability to complex self-assembling structures for potential tissue engineering or in vitro model applications. Statement of SignificanceMolecular self-assembly is widely used for the fabrication of complex functional biomaterials to replace and/or repair any tissue or organ in the body. However, maintaining the stability and corresponding functionality of these kinds of materials in physiological conditions remains a challenge. Chemical cross-linking strategies (natural or synthetic) have been used in an effort to improve their structural integrity. Here we investigate key performance parameters of different cross-linking strategies for stabilising self-assembled materials with potential biomedical applications using a novel protein-peptide co-assembling membrane as proof-of-concept. From the different cross-linkers tested, the natural cross-linker genipin exhibited the best performance. This cross-linker successfully enhanced the mechanical properties of the system enabling the maintenance of the structure in physiological conditions without compromising its bioactivity and biocompatibility. Altogether, we provide a systematic characterization of cross-linking alternatives for self-assembling materials focused on biocompatibility and stability and demonstrate that genipin is a promising alternative for the cross-linking of such materials with a wide variety of potential applications such as in tissue engineering and drug delivery.

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Dynamic peptide libraries for the discovery of supramolecular nanomaterials

Cited by 197 publications

References 44 publications

Tunable Pentapeptide Self‐Assembled β‐Sheet Hydrogels

Tunable Pentapeptide Self‐Assembled β‐Sheet Hydrogels

Chemoenzymatic Synthesis of Polypeptides for Use as Functional and Structural Materials

Cross-linking of a biopolymer-peptide co-assembling system

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