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{"title"=>"Improved Bone Morphogenetic Protein-2 Retention in an Injectable Collagen Matrix Using Bifunctional Peptides", "type"=>"journal", "authors"=>[{"first_name"=>"Paul T.", "last_name"=>"Hamilton", "scopus_author_id"=>"7201998099"}, {"first_name"=>"Michelle S.", "last_name"=>"Jansen", "scopus_author_id"=>"57198040701"}, {"first_name"=>"Sathya", "last_name"=>"Ganesan", "scopus_author_id"=>"55818293100"}, {"first_name"=>"R. Edward", "last_name"=>"Benson", "scopus_author_id"=>"57194870809"}, {"first_name"=>"Robin", "last_name"=>"Hyde-DeRuyscher", "scopus_author_id"=>"6507625457"}, {"first_name"=>"Wayne F.", "last_name"=>"Beyer", "scopus_author_id"=>"57196753190"}, {"first_name"=>"Joseph C.", "last_name"=>"Gile", "scopus_author_id"=>"56134374100"}, {"first_name"=>"Shrikumar A.", "last_name"=>"Nair", "scopus_author_id"=>"7402726241"}, {"first_name"=>"Jonathan A.", "last_name"=>"Hodges", "scopus_author_id"=>"55817593600"}, {"first_name"=>"Hanne", "last_name"=>"Grøn", "scopus_author_id"=>"6603070420"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"pmid"=>"23950987", "sgr"=>"84881342868", "doi"=>"10.1371/journal.pone.0070715", "scopus"=>"2-s2.0-84881342868", "pui"=>"369535523", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "issn"=>"19326203"}, "id"=>"baf26327-744a-3bde-acf6-7ea210a399d6", "abstract"=>"To promote healing of many orthopedic injuries, tissue engineering approaches are being developed that combine growth factors such as Bone Morphogenetic Proteins (BMP) with biomaterial carriers. Although these technologies have shown great promise, they still face limitations. We describe a generalized approach to create target-specific modular peptides that bind growth factors to implantable biomaterials. These bifunctional peptide coatings provide a novel way to modulate biology on the surface of an implant. Using phage display techniques, we have identified peptides that bind with high affinity to BMP-2. The peptides that bind to BMP-2 fall into two different sequence clusters. The first cluster of peptide sequences contains the motif W-X-X-F-X-X-L (where X can be any amino acid) and the second cluster contains the motif F-P-L-K-G. We have synthesized bifunctional peptide linkers that contain BMP-2 and collagen-binding domains. Using a rat ectopic bone formation model, we have injected rhBMP-2 into a collagen matrix with or without a bifunctional BMP-2: collagen peptide (BC-1). The presence of BC-1 significantly increased osteogenic cellular activity, the area of bone formed, and bone maturity at the site of injection. Our results suggest that bifunctional peptides that can simultaneously bind to a growth factor and an implantable biomaterial can be used to control the delivery and release of growth factors at the site of implantation.", "link"=>"http://www.mendeley.com/research/improved-bone-morphogenetic-protein2-retention-injectable-collagen-matrix-using-bifunctional-peptide", "reader_count"=>22, "reader_count_by_academic_status"=>{"Student > Doctoral Student"=>2, "Researcher"=>6, "Student > Ph. D. Student"=>8, "Student > Master"=>3, "Other"=>2, "Student > Bachelor"=>1}, "reader_count_by_user_role"=>{"Student > Doctoral Student"=>2, "Researcher"=>6, "Student > Ph. D. Student"=>8, "Student > Master"=>3, "Other"=>2, "Student > Bachelor"=>1}, "reader_count_by_subject_area"=>{"Engineering"=>5, "Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>3, "Materials Science"=>2, "Agricultural and Biological Sciences"=>5, "Medicine and Dentistry"=>1, "Veterinary Science and Veterinary Medicine"=>1, "Pharmacology, Toxicology and Pharmaceutical Science"=>1, "Chemistry"=>3}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>5}, "Materials Science"=>{"Materials Science"=>2}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Chemistry"=>{"Chemistry"=>3}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>5}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Unspecified"=>{"Unspecified"=>1}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}, "Veterinary Science and Veterinary Medicine"=>{"Veterinary Science and Veterinary Medicine"=>1}}, "group_count"=>2}

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• http://doi.org/10.1016/j.actbio.2015.07.027
• http://doi.org/10.1007/s13346-015-0233-3
• http://doi.org/10.1016/j.circen.2017.02.009
• http://doi.org/10.1016/j.addr.2018.11.004
• http://doi.org/10.1021/acschembio.5b00717
• http://doi.org/10.1517/17425247.2015.993314
• http://doi.org/10.1016/j.circir.2016.07.001
• http://doi.org/10.1039/C7TB02999C
• http://doi.org/10.1016/j.copbio.2016.02.029
• http://doi.org/10.1186/1749-799X-9-18
• http://doi.org/10.1002/jbm4.10172

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/1147967"], "description"=>"<p>rhBMP-2 (2 μg) was delivered in a rat ectopic bone model either alone (no peptide) or in combination with a 50-fold molar excess of the bifunctional peptide (Collagen-BMP peptide). H&E stained slides were scored for osteogenic cellular activity, bone area and bone maturity by two observers and the median score for each group is shown in the figure. ****, p<.0001 vs no peptide.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "rhbmp-2", "delivered", "collagen", "gel", "bifunctional"], "article_id"=>768219, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.g008", "stats"=>{"downloads"=>1, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Ectopic_bone_formation_with_rhBMP_2_delivered_in_a_collagen_gel_with_or_without_the_bifunctional_peptide_/768219", "title"=>"Ectopic bone formation with rhBMP-2 delivered in a collagen gel with or without the bifunctional peptide.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147981"], "description"=>"*<p>Based on 18 sequences. Format is single-letter amino acid code and frequency of occurrence at that position in the peptide.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "bmp-2", "binding", "peptides", "containing", "motif"], "article_id"=>768233, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.t004", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Summary_of_BMP_2_binding_peptides_containing_motif_2_/768233", "title"=>"Summary of BMP-2 binding peptides containing motif 2^*.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147979"], "description"=>"*<p>X can be any of the 20 natural amino acids. Amino acids in brackets [ ] are the restricted set of amino acids allowed in that position in the encoded peptide library.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "motif", "bmp-binding"], "article_id"=>768231, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.t001", "stats"=>{"downloads"=>3, "page_views"=>17, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Focused_library_design_for_motif_1_and_motif_2_BMP_binding_peptides_/768231", "title"=>"Focused library design for motif 1 and motif 2 BMP-binding peptides^*.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147980"], "description"=>"*<p>nd –not determined.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "scores", "observers", "blinded", "samples", "rhbmp-2", "delivered", "collagen", "gel", "bifunctional"], "article_id"=>768232, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.t006", "stats"=>{"downloads"=>0, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Histology_scores_average_from_two_observers_blinded_to_the_study_of_all_samples_with_rhBMP_2_delivered_in_a_collagen_gel_with_or_without_the_bifunctional_peptide_/768232", "title"=>"Histology scores (average from two observers blinded to the study) of all samples with rhBMP-2 delivered in a collagen gel with or without the bifunctional peptide.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147961"], "description"=>"<p>Biotinylated peptides were immobilized on streptavidin-coated plates and incubated with a range of rhBMP-2 concentrations in TBST for 1 h. BMP-2 binding was analyzed using antibody and <i>p</i>-NPP detection. Peptides B-6, B-17, and B-18 had the highest binding affinities for rhBMP-2. Peptide N-1 is a negative control that binds hexokinase. Data are presented as the absorbance read at 405 nm.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "binding"], "article_id"=>768213, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.g004", "stats"=>{"downloads"=>0, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_BMP_2_Binding_to_Peptide_/768213", "title"=>"BMP-2 Binding to Peptide.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147978"], "description"=>"*<p>Based on 41 sequences. Format is single-letter amino acid code and frequency of occurrence at that position in the peptide.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "bmp-2", "binding", "peptides", "containing", "motif"], "article_id"=>768230, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.t003", "stats"=>{"downloads"=>1, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Summary_of_BMP_2_binding_peptides_containing_motif_1_/768230", "title"=>"Summary of BMP-2 binding peptides containing motif 1^*.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147975"], "description"=>"<p><b>A</b>: 2 µg BMP-2 in 1.5% collagen gel and <b>B</b>: 2 µg BMP-2 with 50-fold molar excess of collagen-BMP-2 bifunctional peptide in 1.5% collagen gel. <b>b</b> – Represent regions of bone; <b>c</b> – represent regions of collagen; cells are stained blue. The image shows only cellular activity in sample A, whereas sample B shows bone formation and increased cellular activity.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "histology", "eosin", "ectopic", "2x"], "article_id"=>768227, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.g009", "stats"=>{"downloads"=>1, "page_views"=>19, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Representative_histology_image_hematoxylin_and_eosin_stain_from_the_rat_ectopic_model_obtained_at_a_2X_magnification_/768227", "title"=>"Representative histology image (hematoxylin and eosin stain) from the rat ectopic model obtained at a 2X magnification.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147960"], "description"=>"<p>Biotinylated BMP-2 was immobilized on streptavidin-coated plates and subjected to multiple rounds of phage display selections using the focused libraries. Peptides which contain motif 2 were aligned. Amino acids which are present in over half of the aligned sequences at a given position are highlighted.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "binding", "peptides", "containing", "motif", "selections", "focused"], "article_id"=>768212, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.g003", "stats"=>{"downloads"=>1, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_BMP_2_Binding_Peptides_Containing_Motif_2_Isolated_from_Selections_Using_the_Focused_Libraries_/768212", "title"=>"BMP-2 Binding Peptides Containing Motif 2 Isolated from Selections Using the Focused Libraries.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147965"], "description"=>"<p>A bifunctional peptide (BC-1) was synthesized containing Peptide B-17 and a collagen-binding peptide with a short amino acid linker. rhBMP-2 was mixed with or without the bifunctional peptide and added to a collagen gel. The bifunctional peptide enhanced the retention of rhBMP-2 to the collagen gel (no peptide, EC50 = 5.5 nM; BC-1, EC50 = 0.41 nM). Data are presented as the absorbance read at 405 nm.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "binding", "bmp-2", "injectable"], "article_id"=>768217, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.g007", "stats"=>{"downloads"=>0, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Bifunctional_peptide_8211_mediated_binding_of_BMP_2_to_injectable_collagen_/768217", "title"=>"Bifunctional peptide–mediated binding of BMP-2 to injectable collagen.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147982"], "description"=>"<p>Sequence of consensus BMP-binding peptides.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "bmp-binding"], "article_id"=>768234, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.t005", "stats"=>{"downloads"=>0, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sequence_of_consensus_BMP_binding_peptides_/768234", "title"=>"Sequence of consensus BMP-binding peptides.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147963"], "description"=>"<p>The biotinylated peptides were coated on streptavidin plates and incubated in TBST (<b>A</b>) or plasma (<b>B</b>) with nanomolar concentrations of rhBMP-2 for 1 h. BMP-2 binding was analyzed using antibody and <i>p</i>-NPP detection. The peptides captured more rhBMP-2 from solution than the no peptide control. Data are presented as the absorbance read at 405 nm.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "bmp-2", "spiked", "tbst"], "article_id"=>768215, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.g006", "stats"=>{"downloads"=>0, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Peptide_mediated_capture_of_BMP_2_from_spiked_TBST_or_plasma_/768215", "title"=>"Peptide-mediated capture of BMP-2 from spiked TBST or plasma.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147962"], "description"=>"<p>Peptides B-17 (A) and B-18 (B) were immobilized on a streptavidin-coated plate, and a range of concentrations of growth factors in the TGF-β superfamily were titrated onto the plate in TBST for 1 h. Growth factor binding was analyzed using antibody and <i>p</i>-NPP detection. Both peptide B-17 and B-18 bound to rhBMP-2, rhBMP-6, and rhBMP-7. Peptide B-17 also cross-reacted with rhBMP-3, rhBMP-5, and rhBMP-12. The peptides had lower affinities for all other growth factors tested. Data are presented as the absorbance read at 405 nm.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "cross-reactivity"], "article_id"=>768214, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.g005", "stats"=>{"downloads"=>0, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Peptide_cross_reactivity_to_other_growth_factors_/768214", "title"=>"Peptide cross-reactivity to other growth factors.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147959"], "description"=>"<p>Biotinylated BMP-2 was immobilized on streptavidin-coated plates and subjected to multiple rounds of phage display selections using the focused libraries. Peptides which contain motif 1 were aligned. Amino acids which are present in over half of the aligned sequences at a given position are highlighted.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "binding", "peptides", "containing", "motif", "selections", "focused"], "article_id"=>768211, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.g002", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_BMP_2_Binding_Peptides_Containing_Motif_1_Isolated_from_Selections_Using_the_Focused_Libraries_/768211", "title"=>"BMP-2 Binding Peptides Containing Motif 1 Isolated from Selections Using the Focused Libraries.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147977"], "description"=>"*<p>Implant evaluated at 10× Magnification.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "histological"], "article_id"=>768228, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.t002", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Scoring_system_for_histological_analysis_of_bone_growth_/768228", "title"=>"Scoring system for histological analysis of bone growth.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-08-08 04:18:07"}
• {"files"=>["https://ndownloader.figshare.com/files/1147957"], "description"=>"<p>Biotinylated BMP-2 was immobilized on streptavidin-coated plates and subjected to multiple rounds of phage display selections using 10 different phage display peptide libraries. Individual BMP-binding phage were isolated and the sequence of the BMP-binding peptide deduced from the phage DNA sequence. Alignment of the peptides revealed two general sequence motifs among the peptides: motif 1: W-X-X-F-X-X-L and motif 2: L-X-F-P-L-K. These motifs were used to generate 2^nd generation focused libraries. In addition, representative synthetic peptides were made and tested for binding to BMP-2.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Growth factors", "Recombinant proteins", "biotechnology", "Bioengineering", "Medical devices", "biomaterials", "proteomics", "Synthetic peptide", "Drugs and devices", "binding"], "article_id"=>768210, "categories"=>["Medicine", "Engineering", "Biological Sciences"], "users"=>["Paul T. Hamilton", "Michelle S. Jansen", "Sathya Ganesan", "R. Edward Benson", "Robin Hyde-DeRuyscher", "Wayne F. Beyer", "Joseph C. Gile", "Shrikumar A. Nair", "Jonathan A. Hodges", "Hanne Grøn"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0070715.g001", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_BMP_2_Binding_Peptides_/768210", "title"=>"BMP-2 Binding Peptides.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-08-08 04:18:07"}

PMC Usage Stats | Further Information

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Relative Metric

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F1000Prime