The development of novel peptidomimetics is of significance. Herein we introduce a new class of peptidomimetics termed 'AApeptides' developed by our group. Similar to other peptidomimetics, AApeptides are resistant to preteolytic degradation, and possess limitless potential to introduce chemically diverse functional groups. They can also form stable helical structures in solution, augmenting their potential for peptide secondary structure mimicry. In addition to their synthesis and secondary structures, we will illustrate the functions of AApeptides with a few of their applications. These includes the development of one-bead-one-compound AApeptide combinatorial libraries, which lead to the successful identification of ligands that disrupt Abeta aggregation and target cancer-related proteins.  We will also show that AApeptide can mimic bioactive peptides through rational design and specifically recognize cell surface receptors.  We will further demonstrate that some AApeptides display dual functions by possessing both potent antimicrobial  and anti-inflammatory activities.

AApeptides: Structures and functions

247th National Meeting (2014)

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