Publications by Shauna A Robbennolt

Publications by authors named "Shauna A Robbennolt"

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Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation.

Christopher L Moore , Michael H Huang , Shauna A Robbennolt , Kellen R Voss , Benjamin Combs

Biochemistry

December 2011

Tau protein was scanned for highly amyloidogenic sequences in amphiphilic motifs (X)(n)Z, Z(X)(n)Z (n ≥ 2), or (XZ)(n) (n ≥ 2), where X is a hydrophobic residue and Z is a charged or polar residue. N-Acetyl peptides homologous to these sequences were used to study aggregation. Transmission electron microscopy (TEM) showed seven peptides, in addition to well-known primary nucleating sequences Ac(275)VQIINK (AcPHF6*) and Ac(306)VQIVYK (AcPHF6), formed fibers, tubes, ribbons, or rolled sheets.

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- Shauna A Robbennolt's research focuses on understanding the aggregation behavior of tau protein, which is significant in the context of neurodegenerative diseases such as Alzheimer's.
- Her 2011 study identified various secondary nucleating sequences within tau using amphiphilic motifs, revealing their influence on the kinetics and thermodynamics of tau aggregation.
- Employing techniques like transmission electron microscopy (TEM), Robbennolt demonstrated that several synthesized N-acetyl peptides could form diverse amyloid structures, thereby enhancing the understanding of tau protein aggregation dynamics.

Publications by authors named "Shauna A Robbennolt"

Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation.

Synopsis of recent research by authors named "Shauna A Robbennolt"