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Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly
Herein, we report the rich morphological and conformational versatility of a biologically active peptide (PEP‐1), which follows diverse self‐assembly pathways to form up to six distinct nanostructures and up to four different secondary structures through subtle modulation in pH, concentration and te...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9300061/ https://www.ncbi.nlm.nih.gov/pubmed/34758508 http://dx.doi.org/10.1002/anie.202113403 |
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author | Ghosh, Goutam Barman, Ranajit Mukherjee, Anurag Ghosh, Uttam Ghosh, Suhrit Fernández, Gustavo |
author_facet | Ghosh, Goutam Barman, Ranajit Mukherjee, Anurag Ghosh, Uttam Ghosh, Suhrit Fernández, Gustavo |
author_sort | Ghosh, Goutam |
collection | PubMed |
description | Herein, we report the rich morphological and conformational versatility of a biologically active peptide (PEP‐1), which follows diverse self‐assembly pathways to form up to six distinct nanostructures and up to four different secondary structures through subtle modulation in pH, concentration and temperature. PEP‐1 forms twisted β‐sheet secondary structures and nanofibers at pH 7.4, which transform into fractal‐like structures with strong β‐sheet conformations at pH 13.0 or short disorganized elliptical aggregates at pH 5.5. Upon dilution at pH 7.4, the nanofibers with twisted β‐sheet secondary structural elements convert into nanoparticles with random coil conformations. Interestingly, these two self‐assembled states at pH 7.4 and room temperature are kinetically controlled and undergo a further transformation into thermodynamically stable states upon thermal annealing: whereas the twisted β‐sheet structures and corresponding nanofibers transform into 2D sheets with well‐defined β‐sheet domains, the nanoparticles with random coil structures convert into short nanorods with α‐helix conformations. Notably, PEP‐1 also showed high biocompatibility, low hemolytic activity and marked antibacterial activity, rendering our system a promising candidate for multiple bio‐applications. |
format | Online Article Text |
id | pubmed-9300061 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-93000612022-07-21 Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly Ghosh, Goutam Barman, Ranajit Mukherjee, Anurag Ghosh, Uttam Ghosh, Suhrit Fernández, Gustavo Angew Chem Int Ed Engl Research Articles Herein, we report the rich morphological and conformational versatility of a biologically active peptide (PEP‐1), which follows diverse self‐assembly pathways to form up to six distinct nanostructures and up to four different secondary structures through subtle modulation in pH, concentration and temperature. PEP‐1 forms twisted β‐sheet secondary structures and nanofibers at pH 7.4, which transform into fractal‐like structures with strong β‐sheet conformations at pH 13.0 or short disorganized elliptical aggregates at pH 5.5. Upon dilution at pH 7.4, the nanofibers with twisted β‐sheet secondary structural elements convert into nanoparticles with random coil conformations. Interestingly, these two self‐assembled states at pH 7.4 and room temperature are kinetically controlled and undergo a further transformation into thermodynamically stable states upon thermal annealing: whereas the twisted β‐sheet structures and corresponding nanofibers transform into 2D sheets with well‐defined β‐sheet domains, the nanoparticles with random coil structures convert into short nanorods with α‐helix conformations. Notably, PEP‐1 also showed high biocompatibility, low hemolytic activity and marked antibacterial activity, rendering our system a promising candidate for multiple bio‐applications. John Wiley and Sons Inc. 2021-12-20 2022-01-26 /pmc/articles/PMC9300061/ /pubmed/34758508 http://dx.doi.org/10.1002/anie.202113403 Text en © 2021 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Research Articles Ghosh, Goutam Barman, Ranajit Mukherjee, Anurag Ghosh, Uttam Ghosh, Suhrit Fernández, Gustavo Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly |
title | Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly |
title_full | Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly |
title_fullStr | Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly |
title_full_unstemmed | Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly |
title_short | Control over Multiple Nano‐ and Secondary Structures in Peptide Self‐Assembly |
title_sort | control over multiple nano‐ and secondary structures in peptide self‐assembly |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9300061/ https://www.ncbi.nlm.nih.gov/pubmed/34758508 http://dx.doi.org/10.1002/anie.202113403 |
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