Self-assembly of bio-inspired heterochiral peptides (51 views)
Bioorg Chem (ISSN: 0045-2068linking, 1090-2120electronic), 2021 Sep; 114: 105047-105047.
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Paper type: Journal Article,
Impact factor: 4.831, 5-year impact factor: 3.39
Url: Not available.
Keywords: Compatibilty, Heterochirality, Peptide Hydrogels,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, University of Naples "Federico II", Italy.
Center for Advanced Biomaterial for Health Care (CABHC), Istituto Italiano di Tecnologia, Naples, Italy
Interdisciplinary Research Centre on Biomaterials (CRIB), Department of Ingegneria Chimica del Materiali e della Produzione Industriale (DICMAPI), University "Federico II", Piazzale Tecchio 80, 80125 Naples, Italy.
Institute of Biostructures and Bioimaging - CNR, 80134 Naples, Italy.
Department of Translational Medical Science, University of Naples Federico II, 80131 Napoli, Italy.
References:
Not available.
Bioorg Chem (ISSN: 0045-2068linking, 1090-2120electronic), 2021 Sep; 114: 105047-105047.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.831, 5-year impact factor: 3.39
Url: Not available.
Keywords: Compatibilty, Heterochirality, Peptide Hydrogels,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, University of Naples "Federico II", Italy.
Center for Advanced Biomaterial for Health Care (CABHC), Istituto Italiano di Tecnologia, Naples, Italy
Interdisciplinary Research Centre on Biomaterials (CRIB), Department of Ingegneria Chimica del Materiali e della Produzione Industriale (DICMAPI), University "Federico II", Piazzale Tecchio 80, 80125 Naples, Italy.
Institute of Biostructures and Bioimaging - CNR, 80134 Naples, Italy.
Department of Translational Medical Science, University of Naples Federico II, 80131 Napoli, Italy.
References:
Not available.
Self-assembly of bio-inspired heterochiral peptides
Peptide hydrogels, deriving from natural protein fragments, present unique advantages as compatibility and low cost of production that allow their wide application in different fields as wound healing, cell delivery and tissue regeneration. To engineer new biomaterials, the change of the chirality of single amino acids demonstrated a powerful approach to modulate the self-assembly mechanism. Recently we unveiled that a small stretch spanning residues 268-273 in the C-terminal domain (CTD) of Nucleophosmin 1 (NPM1) is an amyloid sequence. Herein, we performed a systematic D-scan of this sequence and analyzed the structural properties of obtained peptides. The conformational and kinetic features of self-aggregates and the morphologies of derived microstructures were investigated by means of different biophysical techniques, as well as the compatibility of hydrogels was evaluated in HeLa cells. All the investigated hexapeptides formed hydrogels even if they exhibited different conformational intermediates during aggregation, and they structural featured are finely tuned by introduced chiralities.
Peptide hydrogels, deriving from natural protein fragments, present unique advantages as compatibility and low cost of production that allow their wide application in different fields as wound healing, cell delivery and tissue regeneration. To engineer new biomaterials, the change of the chirality of single amino acids demonstrated a powerful approach to modulate the self-assembly mechanism. Recently we unveiled that a small stretch spanning residues 268-273 in the C-terminal domain (CTD) of Nucleophosmin 1 (NPM1) is an amyloid sequence. Herein, we performed a systematic D-scan of this sequence and analyzed the structural properties of obtained peptides. The conformational and kinetic features of self-aggregates and the morphologies of derived microstructures were investigated by means of different biophysical techniques, as well as the compatibility of hydrogels was evaluated in HeLa cells. All the investigated hexapeptides formed hydrogels even if they exhibited different conformational intermediates during aggregation, and they structural featured are finely tuned by introduced chiralities.
Self-assembly of bio-inspired heterochiral peptides
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