Identification of a Highly Specific Hydroxyapatite‐binding Peptide using Phage Display

Roy, Marc D.; Stanley, Scott K.; Amis, Eric J.; Becker, Matthew L.

doi:10.1002/adma.200702322

Cited by 101 publications

(77 citation statements)

References 32 publications

(29 reference statements)

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“…Among nucleating peptides, two types of representative nucleators, a phosphate chelating agent (N6p) or calcium chelating agents (NWp and W6p), were selected. N6p is a reported CaP-binding peptide identified through phage display, and its binding effect is thought to be due to phosphate-chelating domains (SVKRGTSVG and VGMKPSP) (31). NWp is derived from the N-terminal 15-residue fragment of salivary statherin, a CaP high-affinity protein, and it has been used in biomimetic mineralization (32).…”

Section: Resultsmentioning

confidence: 99%

Rational design of thermostable vaccines by engineered peptide-induced virus self-biomineralization under physiological conditions

Wang

Cao

Chen

et al. 2013

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

141

127

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The development of vaccines against infectious diseases represents one of the most important contributions to medical science. However, vaccine-preventable diseases still cause millions of deaths each year due to the thermal instability and poor efficacy of vaccines. Using the human enterovirus type 71 vaccine strain as a model, we suggest a combined, rational design approach to improve the thermostability and immunogenicity of live vaccines by self-biomineralization. The biomimetic nucleating peptides are rationally integrated onto the capsid of enterovirus type 71 by reverse genetics so that calcium phosphate mineralization can be biologically induced onto vaccine surfaces under physiological conditions, generating a mineral exterior. This engineered self-biomineralized virus was characterized in detail for its unique structural, virological, and chemical properties. Analogous to many exteriors, the mineral coating confers some new properties on enclosed vaccines. The self-biomineralized vaccine can be stored at 26°C for more than 9 d and at 37°C for approximately 1 wk. Both in vitro and in vivo experiments demonstrate that this engineered vaccine can be used efficiently after heat treatment or ambient temperature storage, which reduces the dependence on a cold chain. Such a combination of genetic technology and biomineralization provides an economic solution for current vaccination programs, especially in developing countries that lack expensive refrigeration infrastructures.genetic engineering | vaccine design | shell

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Section: Resultsmentioning

confidence: 99%

Rational design of thermostable vaccines by engineered peptide-induced virus self-biomineralization under physiological conditions

Wang

Cao

Chen

et al. 2013

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

141

127

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“…1B). The NE1 peptide (ERKRARLT) contains a stretch of charged residues and is likely to be displayed on the outer surface, whereas N6 is a calcium phosphate-binding peptide identified through phage display, and its binding effect is thought to be mediated by phosphate-chelating domains (SVKRGTSVG and VGMKPSP) (30). The NE1 and N6 peptides are both nucleating peptides that would enhance the capability of phosphate chelating to form a thermostable virus vaccine candidate (2).…”

Section: Generation Of Ev71 Recombinantmentioning

confidence: 99%

Crystal Structures of Enterovirus 71 (EV71) Recombinant Virus Particles Provide Insights into Vaccine Design

Lyu

Wang

et al. 2015

Journal of Biological Chemistry

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Background:No HFMD vaccine is available. Results: Structures of EV71 recombinant virus particles were determined showing that the inserted foreign peptide is exposed on the particle surface without capsid structural changes and that virus uncoating is not affected. Conclusion: VP1 BC loop is suitable for foreign peptide insertion for the generation of recombinant EV71 viruses. Significance: The results provide insights into vaccine development.

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“…They could be derived from native proteins having conserved fragments in different organisms or created by artificial evolution (11). Several groups have used artificial evolutionary systems to identify HA-binding peptides (12)(13)(14). On the other hand, natural peptides are mostly fragments of bone tissue proteins that are known to be involved in the mediation of HA formation.…”

mentioning

confidence: 99%

C-terminal Amidation of an Osteocalcin-derived Peptide Promotes Hydroxyapatite Crystallization

Hosseini

Naderi-Manesh

Mountassif

et al. 2013

Journal of Biological Chemistry

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Background: A natural motif sequence was used as substrate to template hydroxyapatite (HA) formation. Results: HA crystal formation is attributed to C-terminal amidation of a natural peptide derived from osteocalcin. Conclusion: The chemical structure of the peptide controls HA crystal formation and growth. Significance: HA-binding peptides are relevant for biomimetic bone synthesis, hard tissue regeneration, and improvement of osseointegration of biomedical implants.

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Identification of a Highly Specific Hydroxyapatite‐binding Peptide using Phage Display

Cited by 101 publications

References 32 publications

Rational design of thermostable vaccines by engineered peptide-induced virus self-biomineralization under physiological conditions

Rational design of thermostable vaccines by engineered peptide-induced virus self-biomineralization under physiological conditions

Crystal Structures of Enterovirus 71 (EV71) Recombinant Virus Particles Provide Insights into Vaccine Design

C-terminal Amidation of an Osteocalcin-derived Peptide Promotes Hydroxyapatite Crystallization

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