Effect of Phospholipid Membrane on Conformation of Retro-Sequence Amyloid- beeta-Peptide 35-25 and Normal Amyloid-beeta-Peptide 25-35

Author: Masato Kodaka

Source: Protein and Peptide Letters, Volume 8, Number 5, October 2001 , pp. 395-398(4)

Publisher: Bentham Science Publishers

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Abstract:

Negatively-charged phospholipid membrane does not affect the random coil conformation of a non-neurotoxic amyloid-beeta-peptide having a retro-sequence 35-25 (Abeta 35-25), whereas it changes the conformation of a neurotoxic normal-sequence peptide A beeta 25-35 from a random coil to a beeta-sheet-like structure under the same condition. The formation of the ordered structure seems to be closely related to the expression of neurotoxicity.

Keywords: AMYLOID PEPTIDE 35-25; AMYLOID PEPTIDE 25-35; amyloid peptide

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409274

Affiliations: 1: Institute of Molecular and Cell Biology, Tsukuba Center, National Institute of Advanced Industrial Science and Technology, AIST Tsukuba Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.

Publication date: 2001-10-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.