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Accepted (AM)Open Access (License Unspecified), Open
Journal article
Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal
Journal of the American Chemical Society, v 131(51), pp 18218-18219
30 Dec 2009
PMID: 19958029
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The eight-residue alanine oligopeptide Ac-A(4)KA(2)Y-NH(2) (AKY8) was found to form amyloid-like fibrils upon incubation at room temperature in acidified aqueous solution at peptide concentrations >10 mM. The fibril solution exhibits an enhanced vibrational circular dichroism (VCD) couplet in the amide I' band region that is nearly 2 orders of magnitude larger than typical polypeptide/protein signals in this region. The UV-CD spectrum of the fibril solution shows CD in the region associated with the tyrosine side chain absorption. A similar peptide, Ac-A(4)KA(2)-NH(2) (AK7), which lacks a terminal tyrosine residue, does not aggregate. These results suggest a pivotal role for the C-terminal tyrosine residue in stabilizing the aggregation state of this peptide. It is speculated that interactions between the lysine and tyrosine side chains of consecutive strands in an antiparallel arrangement (e.g., cation-pi interactions) are responsible for the stabilization of the resulting fibrils. These results offer considerations and insight regarding the de novo design of self-assembling oligopeptides for biomedical and biotechnological applications and highlight the usefulness of VCD as a tool for probing amyloid fibril formation.
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Details
- Title
- Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal
- Creators
- Thomas J Measey - Drexel UniversityKathryn B Smith - Mount Holyoke CollegeSean M Decatur - Mount Holyoke CollegeLiming Zhao - Mount Holyoke CollegeGuoliang Yang - Mount Holyoke CollegeReinhard Schweitzer-Stenner - Mount Holyoke College
- Publication Details
- Journal of the American Chemical Society, v 131(51), pp 18218-18219
- Publisher
- American Chemical Society; Washington, DC
- Grant note
- R01 GM071793-05 / NIGMS NIH HHS R01 GM071793 / NIGMS NIH HHS R01-GM071793 / NIGMS NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:000273615800014
- Scopus ID
- 2-s2.0-73249133310
- Other Identifier
- 991019167874804721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Chemistry, Multidisciplinary