Amyloid-Like Fibrillary Morphology Originated by Tyrosine-Containing Aromatic Hexapeptides (132 views)
Chemistry (ISSN: 0947-6539linking, 1521-3765electronic), 2018 May 7; 24 (26 ): 6804-6817.
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Paper type: Journal Article,
Impact factor: 5.476, 5-year impact factor: 5.477
Url: Not available.
Keywords: Amyloid Chemistry , Animals , Biocompatible Materials Chemical Synthesis Chemistry Pharmacology , Cho Cells , Cell Survival Drug Effects , Cricetinae , Cricetulus , Molecular Dynamics Simulation , Oligopeptides Chemical Synthesis Chemistry Pharmacology , Protein Structure, Secondary , Rheology , Spectrometry, Fluorescence , Tyrosine Chemistry , X-Ray Diffraction , Md Simulation , Waxs , Nanostructures , Self-Assembling Peptides , Soft Hydrogels,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II" and DFM Scarl, Via Mezzocannone 16, 80134, Naples, Italy.
Institute of Biostructures and Bioimaging (IBB), CNR, Via Mezzocannone 16, 80134, Naples, Italy.
Institute of Crystallography (IC), CNR, Via Amendola 122, 70126, Bari, Italy.
Department of Oral Biology, The Goldschleger School of Dental Medicine, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
References:
Not available.
Chemistry (ISSN: 0947-6539linking, 1521-3765electronic), 2018 May 7; 24 (26 ): 6804-6817.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.476, 5-year impact factor: 5.477
Url: Not available.
Keywords: Amyloid Chemistry , Animals , Biocompatible Materials Chemical Synthesis Chemistry Pharmacology , Cho Cells , Cell Survival Drug Effects , Cricetinae , Cricetulus , Molecular Dynamics Simulation , Oligopeptides Chemical Synthesis Chemistry Pharmacology , Protein Structure, Secondary , Rheology , Spectrometry, Fluorescence , Tyrosine Chemistry , X-Ray Diffraction , Md Simulation , Waxs , Nanostructures , Self-Assembling Peptides , Soft Hydrogels,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II" and DFM Scarl, Via Mezzocannone 16, 80134, Naples, Italy.
Institute of Biostructures and Bioimaging (IBB), CNR, Via Mezzocannone 16, 80134, Naples, Italy.
Institute of Crystallography (IC), CNR, Via Amendola 122, 70126, Bari, Italy.
Department of Oral Biology, The Goldschleger School of Dental Medicine, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.
References:
Not available.
Amyloid-Like Fibrillary Morphology Originated by Tyrosine-Containing Aromatic Hexapeptides
Phenylalanine-based nanostructures have attracted the attention of the material science community for their functional properties. These properties strongly depend on the hierarchic organization of the nanostructure that in turn can be finely tuned by punctual chemical modifications of the building blocks. Herein, we investigate how the partial or the complete replacement of the Phe residues in PEG(8) -(Phe)(6) (PEG(8) -F6) with tyrosines to generate PEG(8) -(Phe-Tyr)(3) (PEG(8) -(FY)3) or PEG(8) -(Tyr)(6) (PEG(8) -Y6) affects the structural/functional properties of the nanomaterial formed by the parental compound. Moreover, the effect of the PEG derivatization was evaluated through the characterization of the peptides without the PEG moiety (Tyr)(6) (Y6) and (Phe-Tyr)(3) ((FY)3). Both PEG(8) -Y6 and PEG(8) -(FY)3 can self-assemble in water at micromolar concentrations in β-sheet-rich nanostructures. However, WAXS diffraction patterns of these compounds present significant differences. PEG(8) -(FY)3 shows a 2D WAXS oriented fiber diffraction profile characterized by the concomitant presence of a 4.7 Å meridional and a 12.5 Å equatorial reflection that are generally associated with cross-β structure. On the other hand, the pattern of PEG(8) -Y6 is characterized by the presence of circles typically observed in the presence of PEG crystallization. Molecular modeling and dynamics provide an atomic structural model of the peptide spine of these compounds that is in good agreement with WAXS experimental data. Gelation phenomenon was only detected for PEG(8) -(FY)3 above a concentration of 1.0 wt % as confirmed by storage (G'≈100 Pa) and loss (G''≈28 Pa) moduli in rheological studies. The cell viability on CHO cells of this soft hydrogel was certified to be 90 % after 24 hours of incubation.
Phenylalanine-based nanostructures have attracted the attention of the material science community for their functional properties. These properties strongly depend on the hierarchic organization of the nanostructure that in turn can be finely tuned by punctual chemical modifications of the building blocks. Herein, we investigate how the partial or the complete replacement of the Phe residues in PEG(8) -(Phe)(6) (PEG(8) -F6) with tyrosines to generate PEG(8) -(Phe-Tyr)(3) (PEG(8) -(FY)3) or PEG(8) -(Tyr)(6) (PEG(8) -Y6) affects the structural/functional properties of the nanomaterial formed by the parental compound. Moreover, the effect of the PEG derivatization was evaluated through the characterization of the peptides without the PEG moiety (Tyr)(6) (Y6) and (Phe-Tyr)(3) ((FY)3). Both PEG(8) -Y6 and PEG(8) -(FY)3 can self-assemble in water at micromolar concentrations in β-sheet-rich nanostructures. However, WAXS diffraction patterns of these compounds present significant differences. PEG(8) -(FY)3 shows a 2D WAXS oriented fiber diffraction profile characterized by the concomitant presence of a 4.7 Å meridional and a 12.5 Å equatorial reflection that are generally associated with cross-β structure. On the other hand, the pattern of PEG(8) -Y6 is characterized by the presence of circles typically observed in the presence of PEG crystallization. Molecular modeling and dynamics provide an atomic structural model of the peptide spine of these compounds that is in good agreement with WAXS experimental data. Gelation phenomenon was only detected for PEG(8) -(FY)3 above a concentration of 1.0 wt % as confirmed by storage (G'≈100 Pa) and loss (G''≈28 Pa) moduli in rheological studies. The cell viability on CHO cells of this soft hydrogel was certified to be 90 % after 24 hours of incubation.
Amyloid-Like Fibrillary Morphology Originated by Tyrosine-Containing Aromatic Hexapeptides
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Amyloid-Like Fibrillary Morphology Originated by Tyrosine-Containing Aromatic Hexapeptides
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Impact Factor: 5.707
View Export to BibTeX Export to EndNote
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Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2001 Sep 28; 276(39): 36613-36623.
Impact Factor: 7.258
View Export to BibTeX Export to EndNote
Cook JA, Krishna MC, Pacelli R, DeGraff W, Liebmann J, Mitchell JB, Russo A, Wink DA
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Br J Cancer (ISSN: 0007-0920, 0007-0920print, 0007-0920linking), 1997 Sep; 76(3): 325-334.
Impact Factor: 2.938
View Export to BibTeX Export to EndNote
Wink DA, Cook JA, Christodoulou D, Krishna MC, Pacelli R, Kim S, DeGraff W, Gamson J, Vodovotz Y, Russo A, Mitchell JB
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Impact Factor: 2.151
View Export to BibTeX Export to EndNote
Wink DA, Cook JA, Pacelli R, DeGraff W, Gamson J, Liebmann J, Krishna MC, Mitchell JB
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Arch Bioch Bioph (ISSN: 0003-9861, 0003-9861linking), 1996 Jul 15; 331(2): 241-248.
Impact Factor: 2.649
View Export to BibTeX Export to EndNote
14 Records (14 excluding Abstracts).
Total impact factor: 60.05 (60.05 excluding Abstracts).
Total 5 year impact factor: 49.502 (49.502 excluding Abstracts).
Total impact factor: 60.05 (60.05 excluding Abstracts).
Total 5 year impact factor: 49.502 (49.502 excluding Abstracts).
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