Atomic force microscopy reveals a dual collagen‐binding activity for the staphylococcal surface protein <scp>SdrF</scp>

Herman‐Bausier, Philippe; Dufrêne, Yves F.

doi:10.1111/mmi.13254

Cited by 22 publications

(20 citation statements)

References 36 publications

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“…6C). Herman-Bausier and Dufrêne had previously demonstrated two distinct binding events/peaks, a weak and a strong peak, are typically observed in ColBD and collagen interactions [30]. In the current study, a weak signature peak of 36 pN and a stronger signature peak of 91 pN were observed in the interaction of Res-ColBD with collagen I (Fig.…”

Section: Resultssupporting

confidence: 70%

Production and Characterization of Recombinant Collagen-Binding Resilin Nanocomposite for Regenerative Medicine Applications

Mikael

Udangawa

Sorci

et al. 2019

Regen. Eng. Transl. Med.

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Development of mechanically stable and multifunctional biomaterials for sensing, repair, and regeneration applications is of great importance. Herein, we investigate the potential of recombinant resilin-like (Res) nanocomposite elastomer as a template biomaterial for regenerative devices such as adhesive bandages or films, electrospun fibers, screws, sutures, and drug delivery vehicles. Exon I (Rec1) from the native resilin gene of Drosophila (CG15920) was fused with collagen-binding domain (ColBD) from Clostridium histolyticum and expressed in Komagataella pastoris (formerly Pichia pastoris). The 100% binding of Resilin-ColBD (Res-ColBD) to collagen I was shown at a 1:1 ratio by mass. Atomic force microscopy results in force mode show a bimodal profile for the ColBD-binding interactions. Moreover, based on the force-volume map, Res-ColBD adhesion to collagen was statistically significantly higher than resilin without ColBD. Lay Summary Designing advanced biomaterials that will not only withstand the repetitive mechanical loading and flexibility of tissues but also retain biochemical and biophysical interactions remains challenging. The combination of physical, biological, and chemical cues is vital for disease regulation, healing, and ultimately complete regeneration of functional human tissues. Resilin is a super elastic and highly resilient natural protein with good biocompatibility but lacks specific biological and chemical cues. Therefore, resilin decorated with collagen I-binding domain is proposed as a functional nanocomposite template biomaterial. Collagen I is an ideal binding target, as it is the most abundant structural protein found in human body including scars that affect unwanted adhesion. Future Work Musculoskeletal-related injuries and disorders are the second largest cause of disabilities worldwide. Significant pain, neurological discomfort, limited mobility, and substantial financial burden are associated with these disorders. Thus, biocompatible materials comprised of resilin with collagen-binding domain, such as films adhesive bandages (films, fiber matts, or hydrogels), sutures, screws and rods, three-dimensional scaffolds, and delivery vehicles, will be designed and evaluated for multiple musculoskeletal-related regeneration applications.

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Section: Resultssupporting

confidence: 70%

Production and Characterization of Recombinant Collagen-Binding Resilin Nanocomposite for Regenerative Medicine Applications

Mikael

Udangawa

Sorci

et al. 2019

Regen. Eng. Transl. Med.

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“…These forces of interaction between aggrecan and the hydrogel slightly increase from 0.97 to 1.25 nN with increasing DS of gel-MA. The forces detected are in the same range compared to the forces detected between proteins and biomaterial surfaces including collagen and hyaluronic acid (Donlon, Nordin, & Frankel, 2012;Herman-Bausier & Dufrene, 2016). …”

mentioning

confidence: 78%

Gelatin- and starch-based hydrogels. Part A: Hydrogel development, characterization and coating

Nieuwenhove

Salamon

Peters

et al. 2016

Carbohydrate Polymers

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The present work aims at constructing the ideal scaffold matrix of which the physico-chemical properties can be altered according to the targeted tissue regeneration application. Ideally, this scaffold should resemble the natural extracellular matrix (ECM) as close as possible both in terms of chemical composition and mechanical properties. Therefore, hydrogel films were developed consisting of methacrylamide-modified gelatin and starch-pentenoate building blocks because the ECM can be considered as a crosslinked hydrogel network consisting of both polysaccharides and structural, signaling and cell-adhesive proteins. For the gelatin hydrogels, three different substitution degrees were evaluated including 31%, 72% and 95%. A substitution degree of 32% was applied for the starch-pentenoate building block. Pure gelatin hydrogels films as well as interpenetrating networks with gelatin and starch were developed. Subsequently, these films were characterized using gel fraction and swelling experiments, high resolution-magic angle spinning (1)H NMR spectroscopy, rheology, infrared mapping and atomic force microscopy. The results indicate that both the mechanical properties and the swelling extent of the developed hydrogel films can be controlled by varying the chemical composition and the degree of substitution of the methacrylamide-modified gelatin applied. The storage moduli of the developed materials ranged between 14 and 63kPa. Phase separation was observed for the IPNs for which separated starch domains could be distinguished located in the surrounding gelatin matrix. Furthermore, we evaluated the affinity of aggrecan for gelatin by atomic force microscopy and radiolabeling experiments. We found that aggrecan can be applied as a bioactive coating for gelatin hydrogels by a straightforward physisorption procedure. Thus, we achieved distinct fine-tuning of the physico-chemical properties of these hydrogels which render them promising candidates for tissue engineering approaches.

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“…SdrG thus appears to be a formidable player in staphylococcal adhesion to Fg-coated medical implants. Examples also exist of Sdr proteins that interact with other extracellular matrix proteins, such as S. epidermidis SdrF that is responsible for its binding to Cn, which involved weak as well as strong bonds (Herman-Bausier and Dufrêne, 2016).…”

Section: Serine-aspartate Repeat Proteins and Clumping Factorsmentioning

confidence: 99%

Binding Strength of Gram-Positive Bacterial Adhesins

Dufrêne

Viljoen

2020

Front. Microbiol.

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Bacterial pathogens are equipped with specialized surface-exposed proteins that bind strongly to ligands on host tissues and biomaterials. These adhesins play critical roles during infection, especially during the early step of adhesion where the cells are exposed to physical stress. Recent single-molecule experiments have shown that staphylococci interact with their ligands through a wide diversity of mechanosensitive molecular mechanisms. Adhesin-ligand interactions are activated by tensile force and can be ten times stronger than classical non-covalent biological bonds. Overall these studies demonstrate that Gram-positive adhesins feature unusual stress-dependent molecular interactions, which play essential roles during bacterial colonization and dissemination. With an increasing prevalence of multidrug resistant infections caused by Staphylococcus aureus and Staphylococcus epidermidis, chemotherapeutic targeting of adhesins offers an innovative alternative to antibiotics.

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Atomic force microscopy reveals a dual collagen‐binding activity for the staphylococcal surface protein SdrF

Cited by 22 publications

References 36 publications

Production and Characterization of Recombinant Collagen-Binding Resilin Nanocomposite for Regenerative Medicine Applications

Production and Characterization of Recombinant Collagen-Binding Resilin Nanocomposite for Regenerative Medicine Applications

Gelatin- and starch-based hydrogels. Part A: Hydrogel development, characterization and coating

Binding Strength of Gram-Positive Bacterial Adhesins

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