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News April 2, 2021 //---Antibody molecules are currently widely used in clinical treatment and scientific research because they can specifically target different targets.
By gathering and assembling anti-single antibody molecules, the binding effect can often be improved.
By gathering and assembling anti-single antibody molecules, the binding effect can often be improved.
In a recent study, the research group of Professor David Baker from the University of Washington designed a new type of antibody "nanocage".
The nanocage consists of two parts: one is a homo-oligomeric protein that binds the antibody, and the other It is the antibody molecule itself.
The protein designed by precise calculation can drive the assembly of antibody molecules in the nanocage, thereby controlling the symmetry and multivalence of the antibody.
The results of functional studies show that the nanocage structure has stronger binding ability to the SARS-CoV-2 spike protein, and its neutralizing ability to pseudovirus has also been proved by experiments.
The relevant results were published in the "Science" magazine.
The nanocage consists of two parts: one is a homo-oligomeric protein that binds the antibody, and the other It is the antibody molecule itself.
The protein designed by precise calculation can drive the assembly of antibody molecules in the nanocage, thereby controlling the symmetry and multivalence of the antibody.
The results of functional studies show that the nanocage structure has stronger binding ability to the SARS-CoV-2 spike protein, and its neutralizing ability to pseudovirus has also been proved by experiments.
The relevant results were published in the "Science" magazine.
(Image source: www.
sciencemag.
org)
sciencemag.
org)
As we all know, antibodies play a central role in biological research and clinical treatment.
The antibody clusters generated by fusing antibody molecules to polymers or linking antibody fragments together can enhance signal transduction.
However, there is still a lack of assembly methods for producing antibody polymers with precise structures and quantities.
.
The antibody clusters generated by fusing antibody molecules to polymers or linking antibody fragments together can enhance signal transduction.
However, there is still a lack of assembly methods for producing antibody polymers with precise structures and quantities.
.
For this problem, Professor Baker and others hope to assemble antibodies into precise structures with different valences and symmetry through advanced technologies in computational biology and protein synthesis.
In this study, the authors developed a method for designing proteins that can position antibody molecules or Fc fragments on the symmetry axis of conventional dihedral and polyhedral architectures.
Such a design can transfer any antibody to a "nanocage" with uniform texture and clear structure, and such assembly may have a significant impact on cell signal transduction.
In this study, the authors developed a method for designing proteins that can position antibody molecules or Fc fragments on the symmetry axis of conventional dihedral and polyhedral architectures.
Such a design can transfer any antibody to a "nanocage" with uniform texture and clear structure, and such assembly may have a significant impact on cell signal transduction.
First of all, the antibody nanocage (AbC) is designed to rigidly fuse the antibody constant domain binding module with the circular oligomer through the helical spacer domain, so that the symmetry axis of the dimeric antibody and the circular oligomer is at a different dihedral or Polyhedron (for example, tetrahedron, octahedron, or icosahedron) architecture.
(Figure 1, Antibody Nanocage Design Scheme)
Afterwards, the researchers optimized the connection region between the connected building blocks to fold into the designed structure, and then expressed the synthetic gene that it encodes in the bacteria.
Among the 48 structural feature designs, 8 components match the design model.
Successful designs include D2 dihedron (three designs), T32 tetrahedron (two designs), O42 octahedron (one design) and I52 icosahedron (two designs) architecture; they contain 2, 6, 12 Or 30 kinds of antibodies.
Among the 48 structural feature designs, 8 components match the design model.
Successful designs include D2 dihedron (three designs), T32 tetrahedron (two designs), O42 octahedron (one design) and I52 icosahedron (two designs) architecture; they contain 2, 6, 12 Or 30 kinds of antibodies.
(Figure 2, Structural feature analysis of antibody nanocage)
Further, the author investigated the influence of antibody nanocage structure on cell signal transduction.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
(Figure 3.
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
In this study, the authors designed a variety of proteins that can promote the formation of antibody nanocages.
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
Original source: Robby Divine, Ha V.
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
(Image source: www.
sciencemag.
org)
sciencemag.
org)
As we all know, antibodies play a central role in biological research and clinical treatment.
The antibody clusters generated by fusing antibody molecules to polymers or linking antibody fragments together can enhance signal transduction.
However, there is still a lack of assembly methods for producing antibody polymers with precise structures and quantities.
.
The antibody clusters generated by fusing antibody molecules to polymers or linking antibody fragments together can enhance signal transduction.
However, there is still a lack of assembly methods for producing antibody polymers with precise structures and quantities.
.
For this problem, Professor Baker and others hope to assemble antibodies into precise structures with different valences and symmetry through advanced technologies in computational biology and protein synthesis.
In this study, the authors developed a method for designing proteins that can position antibody molecules or Fc fragments on the symmetry axis of conventional dihedral and polyhedral architectures.
Such a design can transfer any antibody to a "nanocage" with uniform texture and clear structure, and such assembly may have a significant impact on cell signal transduction.
In this study, the authors developed a method for designing proteins that can position antibody molecules or Fc fragments on the symmetry axis of conventional dihedral and polyhedral architectures.
Such a design can transfer any antibody to a "nanocage" with uniform texture and clear structure, and such assembly may have a significant impact on cell signal transduction.
First of all, the antibody nanocage (AbC) is designed to rigidly fuse the antibody constant domain binding module with the circular oligomer through the helical spacer domain, so that the symmetry axis of the dimeric antibody and the circular oligomer is at a different dihedral or Polyhedron (for example, tetrahedron, octahedron, or icosahedron) architecture.
(Figure 1, Antibody Nanocage Design Scheme)
Afterwards, the researchers optimized the connection region between the connected building blocks to fold into the designed structure, and then expressed the synthetic gene that it encodes in the bacteria.
Among the 48 structural feature designs, 8 components match the design model.
Successful designs include D2 dihedron (three designs), T32 tetrahedron (two designs), O42 octahedron (one design) and I52 icosahedron (two designs) architecture; they contain 2, 6, 12 Or 30 kinds of antibodies.
Among the 48 structural feature designs, 8 components match the design model.
Successful designs include D2 dihedron (three designs), T32 tetrahedron (two designs), O42 octahedron (one design) and I52 icosahedron (two designs) architecture; they contain 2, 6, 12 Or 30 kinds of antibodies.
(Figure 2, Structural feature analysis of antibody nanocage)
Further, the author investigated the influence of antibody nanocage structure on cell signal transduction.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
(Figure 3.
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
In this study, the authors designed a variety of proteins that can promote the formation of antibody nanocages.
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
Original source: Robby Divine, Ha V.
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
For this problem, Professor Baker and others hope to assemble antibodies into precise structures with different valences and symmetry through advanced technologies in computational biology and protein synthesis.
In this study, the authors developed a method for designing proteins that can position antibody molecules or Fc fragments on the symmetry axis of conventional dihedral and polyhedral architectures.
Such a design can transfer any antibody to a "nanocage" with uniform texture and clear structure, and such assembly may have a significant impact on cell signal transduction.
In this study, the authors developed a method for designing proteins that can position antibody molecules or Fc fragments on the symmetry axis of conventional dihedral and polyhedral architectures.
Such a design can transfer any antibody to a "nanocage" with uniform texture and clear structure, and such assembly may have a significant impact on cell signal transduction.
First of all, the antibody nanocage (AbC) is designed to rigidly fuse the antibody constant domain binding module with the circular oligomer through the helical spacer domain, so that the symmetry axis of the dimeric antibody and the circular oligomer is at a different dihedral or Polyhedron (for example, tetrahedron, octahedron, or icosahedron) architecture.
(Figure 1, Antibody Nanocage Design Scheme)
Afterwards, the researchers optimized the connection region between the connected building blocks to fold into the designed structure, and then expressed the synthetic gene that it encodes in the bacteria.
Among the 48 structural feature designs, 8 components match the design model.
Successful designs include D2 dihedron (three designs), T32 tetrahedron (two designs), O42 octahedron (one design) and I52 icosahedron (two designs) architecture; they contain 2, 6, 12 Or 30 kinds of antibodies.
Among the 48 structural feature designs, 8 components match the design model.
Successful designs include D2 dihedron (three designs), T32 tetrahedron (two designs), O42 octahedron (one design) and I52 icosahedron (two designs) architecture; they contain 2, 6, 12 Or 30 kinds of antibodies.
(Figure 2, Structural feature analysis of antibody nanocage)
Further, the author investigated the influence of antibody nanocage structure on cell signal transduction.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
(Figure 3.
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
In this study, the authors designed a variety of proteins that can promote the formation of antibody nanocages.
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
Original source: Robby Divine, Ha V.
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
First of all, the antibody nanocage (AbC) is designed to rigidly fuse the antibody constant domain binding module with the circular oligomer through the helical spacer domain, so that the symmetry axis of the dimeric antibody and the circular oligomer is at a different dihedral or Polyhedron (for example, tetrahedron, octahedron, or icosahedron) architecture.
(Figure 1, Antibody Nanocage Design Scheme)
Afterwards, the researchers optimized the connection region between the connected building blocks to fold into the designed structure, and then expressed the synthetic gene that it encodes in the bacteria.
Among the 48 structural feature designs, 8 components match the design model.
Successful designs include D2 dihedron (three designs), T32 tetrahedron (two designs), O42 octahedron (one design) and I52 icosahedron (two designs) architecture; they contain 2, 6, 12 Or 30 kinds of antibodies.
Among the 48 structural feature designs, 8 components match the design model.
Successful designs include D2 dihedron (three designs), T32 tetrahedron (two designs), O42 octahedron (one design) and I52 icosahedron (two designs) architecture; they contain 2, 6, 12 Or 30 kinds of antibodies.
(Figure 2, Structural feature analysis of antibody nanocage)
Further, the author investigated the influence of antibody nanocage structure on cell signal transduction.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
(Figure 3.
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
In this study, the authors designed a variety of proteins that can promote the formation of antibody nanocages.
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
Original source: Robby Divine, Ha V.
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
Afterwards, the researchers optimized the connection region between the connected building blocks to fold into the designed structure, and then expressed the synthetic gene that it encodes in the bacteria.
Among the 48 structural feature designs, 8 components match the design model.
Successful designs include D2 dihedron (three designs), T32 tetrahedron (two designs), O42 octahedron (one design) and I52 icosahedron (two designs) architecture; they contain 2, 6, 12 Or 30 kinds of antibodies.
Among the 48 structural feature designs, 8 components match the design model.
Successful designs include D2 dihedron (three designs), T32 tetrahedron (two designs), O42 octahedron (one design) and I52 icosahedron (two designs) architecture; they contain 2, 6, 12 Or 30 kinds of antibodies.
(Figure 2, Structural feature analysis of antibody nanocage)
Further, the author investigated the influence of antibody nanocage structure on cell signal transduction.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
(Figure 3.
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
In this study, the authors designed a variety of proteins that can promote the formation of antibody nanocages.
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
Original source: Robby Divine, Ha V.
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
(Figure 2, Structural feature analysis of antibody nanocage)
Further, the author investigated the influence of antibody nanocage structure on cell signal transduction.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
Studies have found that AbC formed by the assembly of antibody molecules targeting death receptors can induce tumor cell apoptosis, and this process is not affected by soluble antibodies or natural ligands.
In addition, the authors also found that the angiogenin pathway signal, CD40 signal transduction and T cell proliferation signals in the recipient cells were significantly enhanced.
The formation of AbC also improves its in vitro neutralization of SARS-CoV-2 pseudovirus.
(Figure 3.
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
In this study, the authors designed a variety of proteins that can promote the formation of antibody nanocages.
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
Original source: Robby Divine, Ha V.
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
(Figure 3.
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
Antibody nanocage promotes signal transmission such as apoptosis and angiogenesis)
In this study, the authors designed a variety of proteins that can promote the formation of antibody nanocages.
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
These proteins can accurately cluster any antibody into a nanocage with a controllable chemical valence and geometric shape.
2, 6, 12 or 30 antibody nanocage structures can be obtained by simply mixing the antibody with the corresponding designed protein, without any covalent modification of the antibody itself.
Based on the above research results, the author hopes that this rapid and robust antibody multimerization assembly method will help future basic research and the development of clinical treatment options.
(Bioon.
com)
Original source: Robby Divine, Ha V.
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
Original source: Robby Divine, Ha V.
Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
Original source: sciencemag. Dang, George Ueda et al.
, sciencemag.
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science 02 Apr 2021: Vol.
372, Issue 6537, eabd9994 DOI: 10.
1126/science.
abd9994
org/content/372/6537/eabd9994?utm_campaign=toc_sci-mag_2021-04-01&et_rid=16764437&et_cid=3721074">Designed proteins assemble antibodies into modular nanocages.
Science
