Peptides having reduced toxicity that stimulate cholesterol efflux

Bielicki, John K.; Johansson, Jan; Danho, Waleed

Peptides having reduced toxicity that stimulate cholesterol efflux

Patent · Tue Aug 16 04:00:00 EDT 2016

OSTI ID:1298004

Bielicki, John K.; Johansson, Jan; Danho, Waleed

The present invention provides a family of non-naturally occurring polypeptides having cholesterol efflux activity that parallels that of full-length apolipoproteins (e.g., Apo AI and Apo E), and having high selectivity for ABCA1 that parallels that of full-length apolipoproteins. Further, the peptides of the invention have little or no toxicity when administered at therapeutic and higher doses. The invention also provides compositions comprising such polypeptides, methods of identifying, screening and synthesizing such polypeptides, and methods of treating, preventing or diagnosing diseases and disorders associated with dyslipidemia, hypercholesterolemia and inflammation.

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE

DOE Contract Number:: AC02-05CH11231

Assignee:: The Regents of the University of California (Oakland, CA)

Patent Number(s):: 9,416,162

Application Number:: 14/216,749

OSTI ID:: 1298004

Country of Publication:: United States

Language:: English

References (10)

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Computational Complexity, Protein Structure Prediction, and the Levinthal Paradox Ngo, J. Thomas; Marks, Joe; Karplus, Martin The Protein Folding Problem and Tertiary Structure Prediction, p. 433-506 https://doi.org/10.1007/978-1-4684-6831-1_14	book	January 1994
Apolipoprotein E: phospholipid binding studies with synthetic peptides from the carboxyl terminus Sparrow, James T.; Sparrow, Doris A.; Fernando, Germain Biochemistry, Vol. 31, Issue 4, p. 1065-1068 https://doi.org/10.1021/bi00119a015	journal	February 1992
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The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum) Pierce, Elizabeth; Xie, Gary; Barabote, Ravi D. Environmental Microbiology, Vol. 10, Issue 10, p. 2550-2573 https://doi.org/10.1111/j.1462-2920.2008.01679.x	journal	July 2008
Characteristics of the amino acids as components of a peptide hormone sequence Rudinger, J.; Parsons, J. A. Peptide Hormones, p. 1-7 https://doi.org/10.1007/978-1-349-02718-7_1	book	January 1976
The C-Terminal Lipid-Binding Domain of Apolipoprotein E Is a Highly Efficient Mediator of ABCA1-Dependent Cholesterol Efflux that Promotes the Assembly of High-Density Lipoproteins Vedhachalam, Charulatha; Narayanaswami, Vasanthy; Neto, Nicole Biochemistry, Vol. 46, Issue 10, p. 2583-2593 https://doi.org/10.1021/bi602407r	journal	March 2007
Effects of l- or d-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic α-helical model peptide on structure and cell selectivity Song, Yun Mi; Yang, Sung-Tae; Lim, Shin Saeng Biochemical and Biophysical Research Communications, Vol. 314, Issue 2, p. 615-621 https://doi.org/10.1016/j.bbrc.2003.12.142	journal	February 2004
Limits of Cooperativity in a Structurally Modular Protein: Response of the Notch Ankyrin Domain to Analogous Alanine Substitutions in Each Repeat Bradley, Christina Marchetti; Barrick, Doug Journal of Molecular Biology, Vol. 324, Issue 2, p. 373-386 https://doi.org/10.1016/S0022-2836(02)00945-2	journal	November 2002
Protein Folding: A Glimpse of the Holy Grail? Berendsen, H. J. C. Science, Vol. 282, Issue 5389, p. 642-643 https://doi.org/10.1126/science.282.5389.642	journal	October 1998

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