Meet Inspiring Speakers and Experts at our 3000+ Global Conference Series Events with over 1000+ Conferences, 1000+ Symposiums
and 1000+ Workshops on Medical, Pharma, Engineering, Science, Technology and Business.

Explore and learn more about Conference Series : World's leading Event Organizer

Back

Laura J Suggs

Laura J Suggs

The University of Texas at Austin, USA

Title: Molecular self-assembly of tissue engineering matrices

Biography

Biography: Laura J Suggs

Abstract

Using a rational design approach, we have implemented a novel class of self-assembling, peptide-based, hydrogel scaffolds with the unique advantages of biologic specificity, hydrolytic degradability and the ability to incorporate cells. Hydrogel scaffolds with biologic specificity have increasingly been explored for use in tissue engineering and regenerative medicine, particularly those that can both self-assemble and mimic the biological features of extracellular matrix. Molecularly engineered structures provide control over cell and tissue behavior that is not possible with traditional polymers. This type of bottom-up approach may serve as a model for the design and optimization of hydrogel scaffolds with relevant bioactivity for use in tissue engineering. The molecules of interest for this work are self-assembling depsipeptides (DPs), also known as ester amides. Our system makes use of two molecular regions: a hydrophobic tail to control assembly and a hydrophilic depsipeptide oligomer which confers biologic activity and degradability. These molecules can self-assemble into different ordered structures including nanoparticles and fibrous, hydrogel scaffolds. The side chains can be varied among a wide range of chemical groups, resulting in a family of molecules with a host of possible bioactivities. Our group has been focused on depsipeptides where the chemical backbone consists of ester substitutions along the backbone of a peptide oligomer. This class of materials may confer certain advantages of peptide mimics while allowing for hydrolytic degradability. The current work reports the synthesis of depsipeptide analogs of the canonical Arginine-Glycine-Aspartic acid (RGD) sequence, a ubiquitous amino acid motif known to bind cell integrins to mediate cell adhesion and interaction with the extracellular matrix (ECM). (Figure. 1) Our results demonstrate the potential of depsipeptides as the basis for self-assembling hydrogel materials with biological function and controlled hydrolytic degradation.