Journal article
HMGA1a Protein Unfolds or Refolds Synthetic DNA–Chromophore Hybrid Polymers: A Chaperone‐Like Behavior
Chembiochem : a European journal of chemical biology, Vol.9(2), pp.304-311
01/25/2008
Handle:
https://hdl.handle.net/2376/107785
PMID: 18067116
Abstract
High group mobility protein, HMGA1a, was found to play a chaperone‐like role in the folding or unfolding of hybrid polymers that contained well‐defined synthetic chromophores and DNA sequences. The synthetic and biological hybrid polymers folded into hydrophobic chromophoric nanostructures in water, but existed as partially unfolded configurations in pH or salt buffers. The presence of HMGA1a induced unfolding of the hybrid DNA–chromophore polymer in pure water, whereas the protein promoted refolding of the same polymer in various pH or salt buffers. The origin of the chaperone‐like properties probably comes from the ability of HMGA1a to reversibly bind both synthetic chromophores and single stranded DNA. The unfolding mechanisms and the binding stoichiometry of protein–hybrid polymers depended on the sequence of the synthetic polymers.
Into the fold. The cancer biomarker HMGA1a protein was found to function like a chaperone for synthetic foldable polymers, and was able to manipulate the nanostructures of the polymers by unfolding and refolding them. This protein switched on either blue or yellow fluorescence depending solution properties; conversely, the polymer behaved as a unique two‐way bioindicator for the cancer biomarker HMGA1a.
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Details
- Title
- HMGA1a Protein Unfolds or Refolds Synthetic DNA–Chromophore Hybrid Polymers: A Chaperone‐Like Behavior
- Creators
- Wei WanWei WangAlexander D. Q Li
- Publication Details
- Chembiochem : a European journal of chemical biology, Vol.9(2), pp.304-311
- Academic Unit
- Department of Chemistry
- Publisher
- WILEY‐VCH Verlag; Weinheim
- Number of pages
- 8
- Grant note
- National Institute of General Medical Sciences (GM065306)
- Identifiers
- 99900546704601842
- Language
- English
- Resource Type
- Journal article