Self-assembled peptide-based hydrogels as scaffolds for anchorage-dependent cells

Zhou, Mi; Smith, Andrew M.; Das, Apurba K.; Hodson, Nigel; Collins, Richard F.; Ulijn, Rein V.; Gough, Julie E.

doi:10.1016/j.biomaterials.2009.01.010

Cited by 639 publications

(622 citation statements)

References 29 publications

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“…Importantly, the vast amount of pH-responsive systems are used to enable controlled release of hydrogel payload rather than used to persue a switch in material properties thereby controlling catheter-guided injection. [ 22 ] Synthetic supramolecular hydrogelators [23][24][25][26][27][28][29] that are held together by directed, noncovalent interactions are proposed to allow for full control of their sol-gel switching behavior under mild conditions using the dynamic nature of the supramolecular interactions. When exploited to the fullest, supramolecular switchable hydrogels systems might be the solution for future clinical catheter-delivery therapies.…”

Section: Introductionmentioning

confidence: 99%

A Fast pH‐Switchable and Self‐Healing Supramolecular Hydrogel Carrier for Guided, Local Catheter Injection in the Infarcted Myocardium

Bastings

Koudstaal

Kieltyka

et al. 2013

Adv Healthcare Materials

277

175

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Minimally invasive intervention strategies after myocardial infarction use state-of-the-art catheter systems that are able to combine mapping of the infarcted area with precise, local injection of drugs. To this end, catheter delivery of drugs that are not immediately pumped out of the heart is still challenging, and requires a carrier matrix that in the solution state can be injected through a long catheter, and instantaneously gelates at the site of injection. To address this unmet need, a pH-switchable supramolecular hydrogel is developed. The supramolecular hydrogel is switched into a liquid at pH > 8.5, with a viscosity low enough to enable passage through a 1-m long catheter while rapidly forming a hydrogel in contact with tissue. The hydrogel has self-healing properties taking care of adjustment to the injection site. Growth factors are delivered from the hydrogel thereby clearly showing a reduction of infarct scar in a pig myocardial infarction model. yield a further rise in mortality and morbidity. [ 1 ] New strategies are aiming at the prevention of the progression of postmyocardial infarction toward heart failure. Catheter-based drug delivery injection approaches [ 2 , 3 ] are substantially less invasive than for example surgical implantation of in vitro engineered tissues, [ 4 ] patches, [ 5 , 6 ] or drug delivery carriers. [ 7 ] Therefore, catheter-injection strategies are the method of choice with regard to clinical applicability. State-of-the-art is the NOGA catheter that enables precise control over the injection location via a special mapping system. [ 8 ] A 3D electromechanical image of the myocardium can be obtained using an ultralow magnetic-fi eld energy source and a sensor-tipped catheter to locate the catheter position. This mapping allows for the accurate identifi cation of normal and infarcted myocardium, and in this way, enables excellent spatial control over the injection of drugs. Generally, the injected drugs are substantially fast removed from the pulsatile heart when not delivered via a solid or gelated carrier material. Therefore, the

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Section: Introductionmentioning

confidence: 99%

A Fast pH‐Switchable and Self‐Healing Supramolecular Hydrogel Carrier for Guided, Local Catheter Injection in the Infarcted Myocardium

Bastings

Koudstaal

Kieltyka

et al. 2013

Adv Healthcare Materials

277

175

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“…From a more-applied perspective, interest in peptide-and protein-based fibrous biomaterials has increased recently because these materials have potential applications in biotechnology and synthetic biology-for example, as scaffolds for 3D cell culture, tissue engineering, and templating the assembly of functional inorganic materials (10)(11)(12)(13). Although natural proteins can and are being used in these areas, much simpler or stripped-down systems are preferable because they reduce complexity, and potentially allow better understanding and control over the folding and assembly processes leading to fiber formation.…”

mentioning

confidence: 99%

“…However, no design process is complete until the structures of the components and their assemblies have been determined to high resolution to afford molecular and, ideally, atomistic descriptions. Although in silico models for several of the above systems have been presented (11,15,16) and structures for amyloid-like assemblies formed from small peptides are being resolved (17,18), there is currently no high-resolution experimental structure for a fibrous biomaterial of de novo design.…”

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confidence: 99%

Cryo-transmission electron microscopy structure of a gigadalton peptide fiber of de novo design

Sharp

Bruning

Mantell

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Nature presents various protein fibers that bridge the nanometer to micrometer regimes. These structures provide inspiration for the de novo design of biomimetic assemblies, both to address difficulties in studying and understanding natural systems, and to provide routes to new biomaterials with potential applications in nanotechnology and medicine. We have designed a self-assembling fiber system, the SAFs, in which two small α-helical peptides are programmed to form a dimeric coiled coil and assemble in a controlled manner. The resulting fibers are tens of nm wide and tens of μm long, and, therefore, comprise millions of peptides to give gigadalton supramolecular structures. Here, we describe the structure of the SAFs determined to approximately 8 Å resolution using cryotransmission electron microscopy. Individual micrographs show clear ultrastructure that allowed direct interpretation of the packing of individual α-helices within the fibers, and the construction of a 3D electron density map. Furthermore, a model was derived using the cryotransmission electron microscopy data and side chains taken from a 2.3 Å X-ray crystal structure of a peptide building block incapable of forming fibers. This was validated using singleparticle analysis techniques, and was stable in prolonged molecular-dynamics simulation, confirming its structural viability. The level of self-assembly and self-organization in the SAFs is unprecedented for a designed peptide-based material, particularly for a system of considerably reduced complexity compared with natural proteins. This structural insight is a unique high-resolution description of how α-helical fibrils pack into larger protein fibers, and provides a basis for the design and engineering of future biomaterials.fibrous proteins | protein design | helical reconstruction | X-ray crystallography

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“…More recently, next generation systems are being modified to introduce functionality, potentially at the expense of homogeneous assembly, as depicted in Fig. 1 [38,39]. This approach generally attempts to mimic the ECM to provide structural and biochemical support to control and augment tissue repair.…”

Section: Functionalisation Of Peptide Materialsmentioning

confidence: 99%

“…For example, the bioactive sequence fmoc-RGD selfassembles into a well ordered p-b nanoscale assembly and a clear hydrogel [44]. However, doping of fmoc-RGD into a system predominantly consisting of fmoc-FF results in the disruption of the ordering of the system but an increase in the biofunctionality [38]. The presentation of RGD has also been observed to be a function of the aromatic sidechains flanking the epitope, where fmoc-RDGF has a greater bioavailability than fmoc-FRGD, possibly through increased rigidity provided by the aromatic residue at the C terminal [45].…”

Section: Functionalisation Of Peptide Materialsmentioning

confidence: 99%

Self-Assembled Peptides: Characterisation and In Vivo Response

Nisbet

Williams

2012

Biointerphases

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The fabrication of tissue engineering scaffolds is a well-established field that has gained recent prominence for the in vivo repair of a variety of tissue types. Recently, increasing levels of sophistication have been engineered into adjuvant scaffolds facilitating the concomitant presentation of a variety of stimuli (both physical and biochemical) to create a range of favourable cellular microenvironments. It is here that self-assembling peptide scaffolds have shown considerable promise as functional biomaterials, as they are not only formed from peptides that are physiologically relevant, but through molecular recognition can offer synergy between the presentation of biochemical and physio-chemical cues. This is achieved through the utilisation of a unique, highly ordered, nano- to microscale 3-D morphology to deliver mechanical and topographical properties to improve, augment or replace physiological function. Here, we will review the structures and forces underpinning the formation of self-assembling scaffolds, and their application in vivo for a variety of tissue types.

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Self-assembled peptide-based hydrogels as scaffolds for anchorage-dependent cells

Cited by 639 publications

References 29 publications

A Fast pH‐Switchable and Self‐Healing Supramolecular Hydrogel Carrier for Guided, Local Catheter Injection in the Infarcted Myocardium

A Fast pH‐Switchable and Self‐Healing Supramolecular Hydrogel Carrier for Guided, Local Catheter Injection in the Infarcted Myocardium

Cryo-transmission electron microscopy structure of a gigadalton peptide fiber of de novo design

Self-Assembled Peptides: Characterisation and In Vivo Response

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