Dendritic-Like Self-assembling Pentapeptide with Potential Applications in Emerging Biotechnologies

In this study a mutated variant of a previously investigated pentapeptide was synthesized and characterized using different analytical methods [1]. Specifically, a single point mutation of phenylalanine residue with tyrosine at the C-terminus was performed and the self-assembling behavior of the modified peptide was accomplished. Notably, at pH 7.4, the tyrosine-modified peptide exhibits a distinctive dendritic pattern, in contrast to the original peptide, which tended to form amorphous aggregates with a spongy texture. This study offers an initial understanding of the significant influence of aromatic amino acid substitutions on the structural properties of peptides and underscores their potential implications for various applications in biotechnology and materials science.