Indraneel Ghosh
Professor, BIO5 Institute
Professor, Chemistry and Biochemistry-Sci
Primary Department
(520) 621-6331
Work Summary
The broad objective of our research program in Bioorganic Chemistry and Chemical Biology is to construct protein therapeutics, protein mimetics, biomaterials, and biosensors. Our research at the University of Arizona is highly multidisciplinary and utilizes techniques in organic synthesis, biochemistry, molecular biology, and a host of physical characterization methods. Our research motto is simple: Unraveling mysteries and Enabling discoveries.
Research Interest
Professor Neel Ghosh, is the Emily Davis and Homer Weed Distinguished Professor ’08 at the University of Arizona. His laboratory is broadly interested in Chemical Biology and Protein Design and Engineering with a focus on developing new tools and methods for advancing human health. The laboratory has a particular current interest in understanding protein kinases and protein-protein interactions and designing new ways to inhibit them in human diseases. Neel Ghosh is also a co-founder and Chief Scientific Officer for Luceome Biotechnologies. Neel received his doctoral degree in 1998 while working with Professor Jean Chmielewski at Purdue University. His doctoral research focused on designing inhibitors of protein-protein interactions and self-replicating peptides. In 1998 he joined Professor Andrew Hamilton and Professor Lynne Regan’s laboratories at Yale University as a joint postdoctoral fellow. At Yale, he discovered the first conditional split-Green Fluorescent Protein, which has been used as a means for measuring protein-protein interactions by many laboratories and the methodology is sometimes called fluorescent protein complementation. In 2001, Neel Ghosh joined the Department of Chemistry and Biochemistry at the University of Arizona as an Assistant Professor and was promoted to Associate Professor and then to the Davis & Weed Chair and Full Professor in 2011. Keywords: Chemistry, Biochemistry, Biomedical Engineering, Cancer


Yao, S., Ghosh, I., Zutshi, R., & Chmielewski, J. (1998). A self-replicating peptide under ionic control. Angewandte Chemie - International Edition in English, 37(4), 478-481.
Ghosh, I., Zhou, M., & Ghosh, I. -. (2007). Quantum dots and peptides: a bright future together. Biopolymers, 88(3).

Nanocrystalline semi-conductor materials, called quantum dots (QDs), exhibit unique optical and spectroscopic properties, which include, broad absorption, narrow and tunable emission, resistance to photobleaching, strong luminescence, and long luminescent lifetimes. These remarkable properties of QDs have resulted in their use as an alternative to both small-molecule and protein fluorophores in innumerable biological applications. The overlap of QDs with the rich chemistry and biology that is characteristic of the peptide arena is an emerging research area. Peptides engineered with appropriate cysteines or histidines have served as ligands for producing water soluble QDs as well as for tagging protein ligands and biosensors to QD surfaces. Incorporation of cell-penetrating peptides on QD surfaces has allowed for the translocation of functionalized QDs into cells for intracellular imaging applications. QDs containing fluorescently labeled peptide substrates have shown utility in the development of novel protease assays. Moreover, QDs-labeled peptides that serve as ligands for cellular receptors provide an alternative to antibody mediated imaging at the whole-cell and single molecule level to study receptor distribution and trafficking. This review highlights the overlap between QD and peptide chemistry and speculates on future research directions.

Gaj, T., Meyer, S. C., & Ghosh, I. (2007). The AviD-tag, a NeutrAvidin/avidin specific peptide affinity tag for the immobilization and purification of recombinant proteins. Protein Expression and Purification, 56(1), 54-61.

PMID: 17697784;Abstract:

The widespread success of affinity tags throughout the biological sciences has prompted interest in developing new and convenient labeling strategies. Affinity tags are well-established tools for recombinant protein immobilization and purification. More recently these tags have been utilized for selective biological targeting towards multiplexed protein detection in numerous imaging applications as well as for drug-delivery. Recently, we discovered a phage-display selected cyclic peptide motif that was shown to bind selectively to NeutrAvidin and avidin but not to the structurally similar streptavidin. Here, we have exploited this selectivity to develop an affinity tag based on the evolved DRATPY moiety that is orthogonal to known Strep-tag technologies. As proof of principle, the divalent AviD-tag (Avidin-Di-tag) was expressed as a Green Fluorescent Protein variant conjugate and exhibited superior immobilization and elution characteristics to the first generation Strep-tag and a monovalent DRATPY GFP-fusion protein analogue. Additionally, we demonstrate the potential for a peptide based orthogonal labeling strategy involving our divalent AviD-tag in concert with existing streptavidin-based affinity reagents. We believe the AviD-tag and its unique recognition properties will provide researchers with a useful new affinity reagent and tool for a variety of applications in the biological and chemical sciences. © 2007 Elsevier Inc. All rights reserved.

Ghosh, I., & Wirth, M. J. (2007). Parsing the motion of single molecules: a novel algorithm for deconvoluting the dynamics of individual receptors at the cell surface.. Science's STKE : signal transduction knowledge environment, 2007(388), pe28.

PMID: 17536098;Abstract:

To truly understand signal transduction, we will ultimately need to understand the dynamics and kinetics of individual proteins as they perform their functions in a single cell. Groundbreaking advances in single-molecule biophysics now allow us to follow the motion of many individual proteins on the cell surface with the use of fluorescent probes, such as quantum dots. However, discriminating the directed movement of single molecules from their natural Brownian motion remains a challenge. A recent paper provides a powerful statistical approach for distinguishing periods of directed motion of individual gamma-aminobutyric acid (GABA) receptors from periods during which they undergo Brownian motion. This new methodology should help single-molecule researchers determine the dynamics of individual proteins participating in signaling cascades.

Stains, C. I., Furman, J. L., Segal, D. J., & Ghosh, I. (2006). Site-specific detection of DNA methylation utilizing mCpG-SEER. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 128(30), 9761-9765.