Abstract:Titanium
(Ti) and titanium alloys have been widely used in the
field of biomedicine. However, the unmatched biomechanics and poor
bioactivities of conventional Ti implants usually lead to insufficient
osseointegration. To tackle these challenges, it is critical to develop
a novel Ti implant that meets the bioadaptive requirements for load-bearing
critical bone defects. Notably, three-dimensional (3D)-printed Ti
implants mimic the microstructure and mechanical properties of natural
bones. Additionally, eco-frie… Show more
“…We made the HT sequence retain an active N-terminus and link it with the KL part by the Gly-Gly-Gly-Gly linker. An appropriate linker can establish steric hindrance to maximizing the binding efficiency of the protruding peptide motif . Collectively, the above results proved that HL retained two independent functions, the SF-binding by the HT motif and the osteogenic capability by the KL motif, laying the foundation for the use of the HL-modified SFm (HL@SFm) in bone regeneration.…”
Peptides can introduce new functions
to biomaterials
but their
immobilization usually relies on inefficient physical adsorption or
tedious chemical conjugation. Using the Bombyx mori silk fibroin (SF) membrane (SFm) as a model biomaterial, here, we
demonstrate a universal strategy for discovering new peptides that
can “stick” to a biomaterial to functionalize it. Specifically,
two peptide motifs, one screened by phage display biopanning for binding
to the biomaterial (i.e., SF) and another derived from an osteogenic
growth factor (i.e., bone morphogenetic protein-2), are fused into
a new chimeric peptide that can bind to SFm for more efficient osteogenesis.
Theoretical simulations and experimental assays confirm that the chimeric
peptide binds to SF with high affinity, facilely achieving its immobilization
onto SFm. The peptide enables SFm to effectively induce osteogenic
differentiation of human mesenchymal stem cells (MSCs) even without
other osteogenic inducers and efficiently stimulate bone regeneration
in a subcutaneous rat model in 8 weeks, even without MSC seeding,
while not causing inflammatory responses. Since biomaterial-binding
peptides can be readily screened using phage display and functional
peptides can be generated from growth factors, our work suggests a
universal strategy for combining them to seek new peptides for binding
and functionalizing biomaterials.
“…We made the HT sequence retain an active N-terminus and link it with the KL part by the Gly-Gly-Gly-Gly linker. An appropriate linker can establish steric hindrance to maximizing the binding efficiency of the protruding peptide motif . Collectively, the above results proved that HL retained two independent functions, the SF-binding by the HT motif and the osteogenic capability by the KL motif, laying the foundation for the use of the HL-modified SFm (HL@SFm) in bone regeneration.…”
Peptides can introduce new functions
to biomaterials
but their
immobilization usually relies on inefficient physical adsorption or
tedious chemical conjugation. Using the Bombyx mori silk fibroin (SF) membrane (SFm) as a model biomaterial, here, we
demonstrate a universal strategy for discovering new peptides that
can “stick” to a biomaterial to functionalize it. Specifically,
two peptide motifs, one screened by phage display biopanning for binding
to the biomaterial (i.e., SF) and another derived from an osteogenic
growth factor (i.e., bone morphogenetic protein-2), are fused into
a new chimeric peptide that can bind to SFm for more efficient osteogenesis.
Theoretical simulations and experimental assays confirm that the chimeric
peptide binds to SF with high affinity, facilely achieving its immobilization
onto SFm. The peptide enables SFm to effectively induce osteogenic
differentiation of human mesenchymal stem cells (MSCs) even without
other osteogenic inducers and efficiently stimulate bone regeneration
in a subcutaneous rat model in 8 weeks, even without MSC seeding,
while not causing inflammatory responses. Since biomaterial-binding
peptides can be readily screened using phage display and functional
peptides can be generated from growth factors, our work suggests a
universal strategy for combining them to seek new peptides for binding
and functionalizing biomaterials.
“…Another peptide TBP-CP05 colonized EVs RGD on the titanium implant surfaces specifically and selectively. 37,38 SEM and AFM showed peptides, EVs and EVs RGD even after being washed with PBS, verifying that the modifying molecules successfully adsorb on the titanium surface. Moreover, it evidenced that EVs RGD has no implication on the characteristics of titanium discs.…”
Titanium (Ti) and its alloys has been universally used as surgical implants, the clinical need for modifying titanium surfaces to accelerate the early stage osseointegration and prevent implant loosening is...
“…5 Q). Combining the above results reveals that the addition of cell sheets consisting of ECM and BMSCs could increase the bone formation promoted by PT scaffolds in the PT/HC and PT/CS groups [ 28 , 43 ]. Fig.…”
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