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The discovery of piezoelectric property of biological materials in human body and their intimate association with human health has spurred new research into development of bio-based piezoelectric platforms for biomedical applications due to their intrinsic biocompatibility, biodegradability, and environmental sustainability. The origin of piezoelectricity in biomaterials arises from the overall molecular dipoles owing to their molecular arrangement at atomic level. Due to low proficiency of piezoelectric biomaterials as compared to inorganic materials and synthetic polymers, proper understanding and controlling the electromechanical response of biomolecular structures is of great interest. Herein, we comprehensively summarize the recent development of concepts and engineering strategies to attune piezoelectric property of biomolecules through artificial manufacturing. Modulation of macroscopic piezoelectricity through alteration of molecular packing and rearrangements of polar domains is discussed. Following the recent state-of-the-art biomedical applications in energy harvesting, biosensing and healthcare monitoring, and tissue engineering are outlined. Finally, the current challenges in design and synthesis of large-scale, efficient piezoelectric artificial biomaterials and possible future research directions have been indicated. We envision that the current review will provide insight in the molecular-level understanding of the piezoelectric effect in biomaterials and pave the way for designing exciting new materials for future medical implants.

Piezoelectric materials which are non-toxic and eco-friendly are of interest. Here, the authors report on the creation of collagen-mimetic peptides which can be self-assembled into piezoelectric materials and study the design characteristics required for optimized power generation.

Summary: Liquid-liquid phase separation (LLPS) of proteins mediates the assembly of biomolecular condensates involved in physiological and pathological processes. Identifying the minimalistic building blocks and the sequence determinant of protein phase separation is an urgent need but remains challenging partially due to lack of methodologies to characterize the phase behavior. Here, we demonstrate computational tools to efficiently quantify the microscopic fluidity of liquid condensates and the temperature-dependent phase diagram of peptides. We comprehensively explore the LLPS abilities of all 400 dipeptide combinations of coded amino acids and observe the occurrences of spontaneous LLPS in three categories of dipeptides. Our predictions are validated by turbidity assays and differential interference contrast (DIC) microscopy. We demonstrate that dipeptides, minimal but complete, possess multivalent interactions sufficient for LLPS, suggesting LLPS is a general property of peptides and proteins, independent of their sequence length. This study paves the way for the prediction and characterization of peptide phase behavior at the molecular level.

DNA is an attractive nanomaterial, yet limited compared to polyamides due to low stability and mechanical issues. Here, the authors combine polyamide and DNA characteristics to form mechanically rigid self-assembled peptide nucleic acid based materials with high stiffness and Young’s modulus.