Document Type
Article
Publication Date
2016
Keywords
Molecular conformation, Oncogene proteins, Protein folding, Structural biology
Digital Object Identifier (DOI)
https://doi.org/10.1038/srep23320
Abstract
Therapeutic insulin, in its native and biosynthetic forms as well as several currently available insulin analogues, continues to be the protein of most interest to researchers. From the time of its discovery to the development of modern insulin analogues, this important therapeutic protein has passed through several stages and product generations. Beside the well-known link between diabetes and cancer risk, the currently used therapeutic insulin analogues raised serious concerns due to their potential roles in cancer initiation and/or progression. It is possible that structural variations in some of the insulin analogues are responsible for the appearance of new oncogenic species with high binding affinity to the insulin-like growth factor 1 (IGF1) receptor. The question we are trying to answer in this work is: are there any specific features of the distribution of intrinsic disorder propensity within the amino acid sequences of insulin analogues that may provide an explanation for the carcinogenicity of the altered insulin protein?
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Scientific Reports, v. 6, art. 23320
Scholar Commons Citation
Redwan, Elrashdy M.; Linjawi, Moustafa H.; and Uversky, Vladimir N., "Looking at the Carcinogenicity of Human Insulin Analogues via the Intrinsic Disorder Prism" (2016). Molecular Medicine Faculty Publications. 332.
https://digitalcommons.usf.edu/mme_facpub/332
