Peptide sequence effects on nanofiber formation, hydration and in-gel protein mobility/activity

点击翻译按钮获取中文摘要

Self-assembling peptide hydrogels, composed of nanofibers with nanoscale dimensions, are becoming recognized as a robust platform for a variety of nanomedicine applications: facilitating axon regeneration, sustaining 3D cellular environment, delivering active proteins and small molecules. Preliminary studies indicate a lack of immune response or initiation of the coagulation cascade to these materials: the mechanisms of which remain unknown. These properties, plus the ability to precisely control the peptide sequence, and thereby incorporate cellular and molecular targeting capabilities, makes self-assembled peptide hydrogels very attractive for nanomedicine applications. However, it remains apparent that the peptide hydrogel interaction with a complex biological milieu has yet to be studied in detail. Through understanding the effects of the peptide composition on gel properties as well as protein interactions, it may be possible to develop these materials for multiple technologies: enzymatically controlled drug delivery, tissue engineering scaffolds to enhance wound healing, high surface area biosensors, cardiovascular grafts, etc.