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pH-sensitivity and Conformation Change of the N-terminal Methacrylated Peptide VK20

Published online by Cambridge University Press:  17 July 2017

Zewang You ,
Marc Behl ,
Candy Löwenberg  and
Andreas Lendlein
Zewang You
Affiliation:
Institute of Biomaterial Science, Helmholtz-Zentrum Geesthacht, Kantstr. 55, 14513Teltow, Germany Institute of Chemistry, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476Potsdam, Germany
Marc Behl
Affiliation:
Institute of Biomaterial Science, Helmholtz-Zentrum Geesthacht, Kantstr. 55, 14513Teltow, Germany
Candy Löwenberg
Affiliation:
Institute of Biomaterial Science, Helmholtz-Zentrum Geesthacht, Kantstr. 55, 14513Teltow, Germany
Andreas Lendlein*
Affiliation:
Institute of Biomaterial Science, Helmholtz-Zentrum Geesthacht, Kantstr. 55, 14513Teltow, Germany Institute of Chemistry, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476Potsdam, Germany
*
*(Email: andreas.lendlein@hzg.de)
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Abstract

N-terminal methacrylation of peptide MAX1, which is capable of conformational changes by variation of the pH, results in a peptide, named VK20. Increasing the reactivity of this terminal group enables further coupling reactions or chemical modifications of the peptide. However, this end group functionalization may influence the ability of conformational changes of VK20, as well as its properties. In this paper, the influence of pH on the transition between random coil and ß-sheet conformation of VK20, including the transition kinetics, were investigated. At pH values of 9 and higher, the kinetics of ß-sheet formation increased for VK20, compared to MAX1. The self-assembly into ß-sheets recognized by the formation of a physically crosslinked gel was furthermore indicated by a significant increase of G’. An increase in pH (from 9 to 9.5) led to a faster gelation of the peptide VK20. Simultaneously, G’ was increased from 460 ± 70 Pa (at pH 9) to 1520 ± 180 Pa (at pH 9.5). At the nanoscale, the gel showed a highly interconnected fibrillary network structure with uniform fibril widths of approximately 3.4 ± 0.5 nm (N=30). The recovery of the peptide conformation back to random coil resulted in the dissolution of the gel, whereby the kinetics of the recovery depended on the pH. Conclusively, the ability of MAX1 to undergo conformational changes was not affected by N-terminal methacrylation whereas the kinetics of pH-sensitive ß-sheet formations has been increased.

Keywords

biomaterialself-assemblykinetics
Type
Articles
Information
MRS Advances , Volume 2 , Issue 47: Soft Materials and Biomaterials , 2017 , pp. 2571 - 2579
Copyright
Copyright © Materials Research Society 2017 

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