Smart Poly(imidazoyl-l-lysine): Synthesis and Reversible Helix-to-Coil Transition at Neutral pH
Polypeptide polymers can adopt natural protein secondary structures such as α-helices or β-sheets, and this unique feature is at the origin of some intriguing physico–chemical properties. In this work, we present how side chain imidazoylation of a poly(l-lysine) scaffold affords the preparation of p...
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doaj-e967cdd20c08450a89dd78b2068204192020-11-25T00:56:22ZengMDPI AGPolymers2073-43602017-07-019727610.3390/polym9070276polym9070276Smart Poly(imidazoyl-l-lysine): Synthesis and Reversible Helix-to-Coil Transition at Neutral pHEstefania Piedra-Arroni0Fatma Makni1Laura Severac2Jean-Luc Stigliani3Geneviève Pratviel4Colin Bonduelle5CNRS, LCC (Laboratoire de Chimie de Coordination (UPR8241)), 205 route de Narbonne, F-31077 Toulouse 31400, FranceCNRS, LCC (Laboratoire de Chimie de Coordination (UPR8241)), 205 route de Narbonne, F-31077 Toulouse 31400, FranceCNRS, LCC (Laboratoire de Chimie de Coordination (UPR8241)), 205 route de Narbonne, F-31077 Toulouse 31400, FranceCNRS, LCC (Laboratoire de Chimie de Coordination (UPR8241)), 205 route de Narbonne, F-31077 Toulouse 31400, FranceCNRS, LCC (Laboratoire de Chimie de Coordination (UPR8241)), 205 route de Narbonne, F-31077 Toulouse 31400, FranceCNRS, LCC (Laboratoire de Chimie de Coordination (UPR8241)), 205 route de Narbonne, F-31077 Toulouse 31400, FrancePolypeptide polymers can adopt natural protein secondary structures such as α-helices or β-sheets, and this unique feature is at the origin of some intriguing physico–chemical properties. In this work, we present how side chain imidazoylation of a poly(l-lysine) scaffold affords the preparation of poly(histidine) counterparts exhibiting α-helix conformation. This structuring behavior is reversible and can be controlled by means of pH and or temperature changes.https://www.mdpi.com/2073-4360/9/7/276smart polypeptidesimidazole-containing polymershelix-to-coil transitionpoly(lysine)pH-responsive |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Estefania Piedra-Arroni Fatma Makni Laura Severac Jean-Luc Stigliani Geneviève Pratviel Colin Bonduelle |
spellingShingle |
Estefania Piedra-Arroni Fatma Makni Laura Severac Jean-Luc Stigliani Geneviève Pratviel Colin Bonduelle Smart Poly(imidazoyl-l-lysine): Synthesis and Reversible Helix-to-Coil Transition at Neutral pH Polymers smart polypeptides imidazole-containing polymers helix-to-coil transition poly(lysine) pH-responsive |
author_facet |
Estefania Piedra-Arroni Fatma Makni Laura Severac Jean-Luc Stigliani Geneviève Pratviel Colin Bonduelle |
author_sort |
Estefania Piedra-Arroni |
title |
Smart Poly(imidazoyl-l-lysine): Synthesis and Reversible Helix-to-Coil Transition at Neutral pH |
title_short |
Smart Poly(imidazoyl-l-lysine): Synthesis and Reversible Helix-to-Coil Transition at Neutral pH |
title_full |
Smart Poly(imidazoyl-l-lysine): Synthesis and Reversible Helix-to-Coil Transition at Neutral pH |
title_fullStr |
Smart Poly(imidazoyl-l-lysine): Synthesis and Reversible Helix-to-Coil Transition at Neutral pH |
title_full_unstemmed |
Smart Poly(imidazoyl-l-lysine): Synthesis and Reversible Helix-to-Coil Transition at Neutral pH |
title_sort |
smart poly(imidazoyl-l-lysine): synthesis and reversible helix-to-coil transition at neutral ph |
publisher |
MDPI AG |
series |
Polymers |
issn |
2073-4360 |
publishDate |
2017-07-01 |
description |
Polypeptide polymers can adopt natural protein secondary structures such as α-helices or β-sheets, and this unique feature is at the origin of some intriguing physico–chemical properties. In this work, we present how side chain imidazoylation of a poly(l-lysine) scaffold affords the preparation of poly(histidine) counterparts exhibiting α-helix conformation. This structuring behavior is reversible and can be controlled by means of pH and or temperature changes. |
topic |
smart polypeptides imidazole-containing polymers helix-to-coil transition poly(lysine) pH-responsive |
url |
https://www.mdpi.com/2073-4360/9/7/276 |
work_keys_str_mv |
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1725227597228408832 |