Sarah Bondos, PhD
Associate Professor
Contact
Medical Physiology
4417 Medical Research Education Building II
Bryan,
TX
77807
bondos@tamu.edu
Phone: 979.436.0807
Fax: 979.847.9481
Biography
My laboratory works in two research areas. First, we are combining biophysical and genetic approaches to understand how proteins use unstructured regions to sense cellular information and respond by adjusting their function. We developed methods to purify Ultrabithorax, a full-length, active Hox transcription factor, and have used this unique opportunity to investigate the role of intramolecular regulatory interactions in tissue-specific protein regulation. Second, we discovered methods to self-assemble Ultrabithorax into robust, extensible materials that are biocompatible and provide unique opportunities for functionalization. These materials are being developed for use as biosensors and to pattern and instruct vascularization in tissue engineering scaffolds.Education and Training
- University of North Carolina, BS, 1993
- University of Illinois, PhD, 1998
Research Interests
- Tissue-specific regulation of protein function During animal development, the Hox transcription factor family determines the identity and guides the formation of many different types of tissues. Because individual members of the Hox protein family define drive the development of multiple types of tissues and organs, each Hox protein must be able to infer their location within the animal and specifically and reliably respond by regulating the appropriate subset of target genes. Misregulation of this process can lead to abnormalities or death in developing animals, or promote carcinogenesis and impede wound repair in adults. Our lab is determining how regions outside the DNA-binding homeodomain of the Drosophila Hox protein Ultrabithroax (Ubx) enhance DNA binding specificity and respond to conformational changes, tissue-specific alternative splicing, protein interactions, and cell signaling cascades. Many of these regulatory mechanisms involve intramolecular interactions between the structured homeodomain and intrinsically disordered (unstructured) regions of the Ubx. We are exploring these mechanisms in vitro and in vivo using a combination of biophysical, cell biological, and genetic approaches.
- Functionalizable protein-based materials We have also developed methods self-assemble Ubx protein into novel biomaterials. These materials hierarchically self-associate into structures ranging from nanoscale fibrils to macroscale fibers, films, and meshes. Because Ubx self-assembles in mild aqueous buffers, we can use standard molecular biology techniques to create fusion proteins, in which a single polypetide encompasses the sequence of Ubx and a functional protein. These fusion proteins are capable of both self-assembly and the function of interest, and thus represent a facile method to functionalize and pattern materials. Ubx materials also bind DNA and nanoparticles, further expanding the range of functionalities that can be incorporated into these materials. We are currently developing Ubx materials as tissue engineering scaffolds and biosensors. Graduate training is available through the Medical Science PhD program(School of Medicine), through the MD/PhD program (School of Medicine) and other programs that our faculty are affiliated with joint research.
Awards, Recognition and Service
- Faculty Early Career Development (CAREER) Program conferred by National Science Foundation - (Arlington, Virginia, United States)
Representative Publications
Lab Members
Graduate Research Assistants
- Amanda Jons
Undergraduate Students
- Brandon Lookfong
- Max Lara