Effect of temperature on self-assembly of an ionic tetrapeptide |
| |
Authors: | M R Tiné M Alderighi C Duce L Ghezzi R Solaro |
| |
Institution: | (1) Department of Chemistry and Industrial Chemistry, University of Pisa, Via Risorgimento 35, 56126 Pisa, Italy |
| |
Abstract: | The self-aggregation of the ionic tetrapeptide RWDW (R = arginine, W = tryptophan, D = aspartic acid) was studied at three
temperatures (15, 25 and 35 °C) by different experimental techniques such as atomic force microscopy (AFM), isothermal titration
calorimetry (ITC) and differential scanning calorimetry (DSC). AFM was used to investigate the morphology of the aggregates;
the AFM images at 15 °C showed the presence of a dense network of entangled fibres, while at 35 °C the peptide assembled into
sparse globular and fibrillar structures. Moreover, the calorimetric experiments showed that in all cases the disaggregation
process is endothermic and dependent on the investigated temperature. Both the enthalpy of disaggregation and the cac change
with temperature. In particular, at 35 °C, we obtained the lower enthalpy of disaggregation and higher cac, showing that the
disaggregation process is favoured at high temperature. The DSC scans strengthen the hypothesis that the RWDW aggregation
is a rather complex phenomenon. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|