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  Polymerizing properties of pepstatin A

Mothes, E., Shoeman, R. L., Schröder, R. R., & Traub, P. (1990). Polymerizing properties of pepstatin A. Journal of Structural Biology, 105(1-3), 80-91. doi:10.1016/1047-8477(90)90102-I.

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 Creators:
Mothes, Elfriede, Author
Shoeman, Robert L.1, 2, 3, Author              
Schröder, Rasmus R.2, 4, Author              
Traub, Peter5, Author              
Affiliations:
1Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society, ou_1497692              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
3Analytical Protein Biochemistry, Max Planck Institute for Medical Research, Max Planck Society, ou_1497690              
4Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
5Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 Abstract: Pepstatin A, a pentapeptide aspartyl protease inhibitor, can spontaneously polymerize into filaments having a helical substructure and, after negative staining, characteristic diameters ranging from 6 to 12 nm. Optical diffraction analysis demonstrated that these filaments consist of a 6-nm-wide strand helically wound with a periodic pitch of 25 nm. Selected images suggest that these filaments may actually be composed of two, intertwined 6-nm-wide strands, an hypothesis not at variance with the diffraction data. These filaments may extend over several micrometers. At low ionic strength and neutral pH, the critical concentration for pepstatin A filament assembly is 0.1 mM. At higher pepstatin A concentrations or in physiological salt solutions, a variety of higher order structures were observed, including ribbons, sheets, and cylinders with both regular and twisted or irregular geometries. Pepstatin A polymerized into these higher order structures loses its ability to inhibit the aspartyl protease of the human immunodeficiency virus type 1. These results have implications not only for model studies on the polymerization of small peptides into higher order structures, but also for the practical development of soluble protease inhibitors.

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Language(s): eng - English
 Dates: 1990-10-241990-09-031990-10-242004-11-301990-12
 Publication Status: Published in print
 Pages: 12
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 Rev. Type: Peer
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Title: Journal of Structural Biology
  Abbreviation : J. Struct. Biol.
Source Genre: Journal
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Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 105 (1-3) Sequence Number: - Start / End Page: 80 - 91 Identifier: ISSN: 1047-8477
CoNE: https://pure.mpg.de/cone/journals/resource/954922650160