4.7 Article Proceedings Paper

Investigation of the self-assembly of hydrophobic self-complementary ionic tetrapeptides

Journal

JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY
Volume 97, Issue 3, Pages 791-796

Publisher

SPRINGER
DOI: 10.1007/s10973-009-0277-z

Keywords

Atomic force microscopy; Isothermal titration calorimetry; Oligopeptide; Self-assembly

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The self-aggregation of two short ionic tetrapeptides (RWDW and RVDV, where R = arginine, V = valine, W = tryptophan, D = aspartic acid) was studied by different experimental techniques such as, atomic force microscopy (AFM), light scattering (LS), isothermal titration calorimetry (ITC) and viscosimetry. AFM was used to investigate the morphology of the aggregates; the AFM images showed the presence of fibrillar aggregates whose number and length increased with increasing oligopeptides concentration. On the other hand, the collected experimental calorimetric and physical chemical results consistently indicated a critical aggregation concentration (cac) around 0.5 and 2.0 mM for RWDW and RVDV respectively.

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