Branched peptides for the modulation of protein-protein interactions: More arms are better than one? (953 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2011 Jun; 18(16): 2429-2437.
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Paper type: Journal Article,
Impact factor: 4.859, 5-year impact factor: 4.806
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79957946154&partnerID=40&md5=217b1041fdbe4141be5b25db8e55c835
Keywords: Combinatorial Peptide Library, Cripto, Fc Receptor, Hepatitis B Virus, Immunoglobulin Purification, Interleukin-6, Map (mulptiple Antigen Peptide), Multimeric Peptides, Neurotensin, Pam (protein A Mimetic), Squamous Cell Carcinoma Antigen 1, Tnfα, Vegfr-1, Growth Factor, Growth Factor Receptor, Protein A Mimetic Peptide, Tripeptide, Unclassified Drug, Vasculotropin Receptor 1, Affinity Chromatography, Amino Acid Sequence, Angiogenesis, Article, Binding Affinity, Cell Differentiation, Cell Fate, Embryonic Stem Cell, Nonhuman, Protein Multimerization, Protein Protein Interaction, Protein Stability, Protein Structure, Systemic Lupus Erythematosus, Animals, Combinatorial Chemistry Techniques, Molecular Structure, Oligopeptides, Protein Binding,
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone, 16, 80134, Napoli, Italy
Angiogenesis Lab, Institute of Genetics and Biophysic Adriano Buzzati-Traverso, CNR, Via Pietro Castellino, 111, 80131 Napoli, Italy
References:
Not available.
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2011 Jun; 18(16): 2429-2437.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.859, 5-year impact factor: 4.806
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79957946154&partnerID=40&md5=217b1041fdbe4141be5b25db8e55c835
Keywords: Combinatorial Peptide Library, Cripto, Fc Receptor, Hepatitis B Virus, Immunoglobulin Purification, Interleukin-6, Map (mulptiple Antigen Peptide), Multimeric Peptides, Neurotensin, Pam (protein A Mimetic), Squamous Cell Carcinoma Antigen 1, Tnfα, Vegfr-1, Growth Factor, Growth Factor Receptor, Protein A Mimetic Peptide, Tripeptide, Unclassified Drug, Vasculotropin Receptor 1, Affinity Chromatography, Amino Acid Sequence, Angiogenesis, Article, Binding Affinity, Cell Differentiation, Cell Fate, Embryonic Stem Cell, Nonhuman, Protein Multimerization, Protein Protein Interaction, Protein Stability, Protein Structure, Systemic Lupus Erythematosus, Animals, Combinatorial Chemistry Techniques, Molecular Structure, Oligopeptides, Protein Binding,
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone, 16, 80134, Napoli, Italy
Angiogenesis Lab, Institute of Genetics and Biophysic Adriano Buzzati-Traverso, CNR, Via Pietro Castellino, 111, 80131 Napoli, Italy
References:
Not available.
Branched peptides for the modulation of protein-protein interactions: More arms are better than one?
Combinatorial peptide libraries from synthetic or biological sources have been largely used in the last two-decades with the aim of identifying bioactive peptides that specifically bind proteins and modulate their interactions with other protein partners. Differently from biological libraries, synthetic methods allow the development of different kinds of libraries based on two main characteristics: i) the use of building blocks and chemical bonds different from those naturally occurring and ii) the possibility of designing scaffolds with non-linear shapes, as cyclic and branched structures. These two features, alone or in combination, have increased the chemical and structural diversity of peptide libraries expanding the offer of collections for the screenings. Here we describe our and other experiences with branched peptides and the results obtained in the last fifteen years. These clearly indicate how the use of short multimerized peptides can represent a successful approach for different applications ranging from affinity chromatography to the modulation of protein-protein interactions in different biological contexts. © 2011 Bentham Science Publishers Ltd.
Combinatorial peptide libraries from synthetic or biological sources have been largely used in the last two-decades with the aim of identifying bioactive peptides that specifically bind proteins and modulate their interactions with other protein partners. Differently from biological libraries, synthetic methods allow the development of different kinds of libraries based on two main characteristics: i) the use of building blocks and chemical bonds different from those naturally occurring and ii) the possibility of designing scaffolds with non-linear shapes, as cyclic and branched structures. These two features, alone or in combination, have increased the chemical and structural diversity of peptide libraries expanding the offer of collections for the screenings. Here we describe our and other experiences with branched peptides and the results obtained in the last fifteen years. These clearly indicate how the use of short multimerized peptides can represent a successful approach for different applications ranging from affinity chromatography to the modulation of protein-protein interactions in different biological contexts. © 2011 Bentham Science Publishers Ltd.
Branched peptides for the modulation of protein-protein interactions: More arms are better than one?
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Branched peptides for the modulation of protein-protein interactions: More arms are better than one?
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
Zaccaro L, Bucci E, Vitale RM, Perretta G, Fattorusso R, Benedetti E, Saviano M, Pedone C
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Impact Factor: 1.377
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 7.258
View Export to BibTeX Export to EndNote
De Falco S, Ruvo M, Verdoliva A, Scarallo A, Raimondo D, Raucci A, Fassina G
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J Pept Res (ISSN: 1397-002x, 1397-002xlinking), 2001 May; 57(5): 390-400.
Impact Factor: 1.522
View Export to BibTeX Export to EndNote
16 Records (15 excluding Abstracts).
Total impact factor: 113.421 (112.044 excluding Abstracts).
Total 5 year impact factor: 85.696 (83.981 excluding Abstracts).
Total impact factor: 113.421 (112.044 excluding Abstracts).
Total 5 year impact factor: 85.696 (83.981 excluding Abstracts).
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