期刊
ACS NANO
卷 11, 期 10, 页码 9825-9835出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.7b03150
关键词
matrix metalloproteinase; triple helix; fibrosis; inflammation; bone formation; targeted delivery
类别
资金
- National Institutes of Health (ORIP) [R43OD021986]
- National Institutes of Health
- Department of Defense (NIH) [R01AR060484, R21AR065124, DOD W81XWH-12-1-0555]
Collagen, the major structural component of nearly all mammalian tissues, undergoes extensive proteolytic remodeling during, developmental states and a variety of life-threatening diseases such as cancer, myocardial infarction, and fibrosis. While degraded collagen could be an important marker of tissue damage, it is difficult to detect and target using conventional tools. Here; we show that a designed peptide (collagen hybridizing peptide: CHP), which specifically hybridizes to the degraded, unfolded collagen chains, can be used to image degraded collagen and inform tissue remodeling activity in various tissues: labeled with 5-carboxyfluorescein and biotin, CHPs enabled direct localization and quantification of collagen degradation in isolated tissues within pathologic states ranging from osteoarthritis and myocardial infarction to glomerulonephritis and pulmonary fibrosis, as well as in normal tissues during developmental programs associated with embryonic bone formation and skin aging. The results indicate the general correlation between the level of collagen remodeling and the amount of denatured collagen in tissue and show that the CHP probes can be used across species and collagen types, providing a versatile tool for not only pathology and developmental biology research but also histology based disease diagnosis, staging, and therapeutic screening. This study lays the foundation for further testing CHP as a targeting moiety for theranostic delivery in various animal models.
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