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(12) United States Patent (10) Patent N0.: US 8,748,569 B2 Stupp Et A] USOO8748569B2 (12) United States Patent (10) Patent N0.: US 8,748,569 B2 Stupp et a]. (45) Date of Patent: Jun. 10, 2014 (54) PEPTIDE AMPHIPHILES AND METHODS TO Berendsen, A Glimpae of the Holy Grail?, Science, 1998, 282, pp. ELECTROSTATICALLY CONTROL 642-643.* BIOACTIVITY OF THE IKVAV PEPTIDE Voet et al, Biochemistry, John Wiley & Sons Inc., 1995, pp. 235 EPITOPE 241.* Ngo et al, Computational Complexity, Protein Structure Protection, (75) Inventors: Samuel I. Stupp, Chicago, IL (US); and the Levinthal Paradox, 1994, pp. 491-494.* Bradley et al., Limits of Cooperativity in a Structurally Modular Joshua E. Goldberger, Columbus, OH Protein: Response of the Notch Ankyrin Domain to Analogous (US); Eric J. Berns, Chicago, IL (US) Alanine Substitutions in Each Repeat, J. M01. BIoL (2002) 324, 373-386.* (73) Assignee: Northwestern University, Evanston, IL Tysseling et al., “Self-assembling peptide amphiphile promotes plas (Us) ticity of serotonergic ?bers following spinal cord injury,” J Neurosci Res, 2010, 88: 3161-3170. ( * ) Notice: Subject to any disclaimer, the term of this Tysseling-Mattiace et al., “Self-assembling nano?bers inhibit glial patent is extended or adjusted under 35 scar formation and promote axon elongation after spinal cord injury,” U.S.C. 154(b) by 0 days. JNeurosci, 2008, 28: 3814-3823. Wheeler et al., “Microcontact printing for precise control of nerve (21) Appl.No.: 13/442,210 cell growth in culture,” J Biomech Eng, 1999, 121: 73-78. Yamada et al., “Ile-Lys-Val-Ala-Val (IKVAV)-containing laminin (22) Filed: Apr. 9, 2012 alphal chain peptides form amyloid-like ?brils,” FEBS Lett, 2002, 530: 48-52. (65) Prior Publication Data Yeung et al., “Modulation of the growth and guidance of rat brain stem neurons using patterned extracellular matrix proteins,” US 2012/0294902 A1 Nov. 22,2012 Neurosci Lett, 2001, 301: 147-150. Yoshida et al., “Identi?cation of a heparin binding site and the bio logical activities of the laminin alphal chain carboxy-terminal globu Related US. Application Data lar domain,” JCell Physiol, 1999, 179: 18-28. Zhang et al., “Compatibility of neural stem cells With functionalized (60) Provisional application No. 61/473,593, ?led on Apr. self-assembling peptide scaffold in vitro,” Biotech Bioprocess Engi 8,2011. neering, 2010, 15: 545-551. Zou et al., “Growth of rat dorsal root ganglion neurons on a novel (51) 1111.0. self-assembling scaffold containing IKVAV sequence,” Mater Sci A61K38/02 (2006.01) Engineering: C, 2009, 29(7)o: 2099-2103. C07K2/00 (2006.01) Zustiak et al., “In?uence of cell-adhesive peptide ligands on poly A61K38/00 (2006.01) (ethylene glycol) hydrogel physical, mechanical and transport prop A61K 9/51 (2006.01) erties,” Acta Biomater, 2010, 6: 3404-3414. B82Y5/00 (2011.01) Adams et al., “Growth cones turn and migrate up an immobilized gradient of the laminin IKVAV peptide,” J Neurobiol, 2005, 62: 134 (52) U.S.Cl. 147. CPC . A61K38/00 (2013.01); C07K2/00 (2013.01); Agheli et al., “Large area protein nanopatterning for biological appli C07K 2319/735 (2013.01); A61K 9/5169 cations,” Nano Lett, 2006, 6: 1165-1171. (2013.01); B82Y5/00 (2013.01); YIOS 977/795 Agius et al., “Antibodies directed against the beta l-integrin subunit (2013.01) and peptides containing the IKVAV sequence of laminin perturb USPC .......................... .. 530/300; 530/345; 977/795 neurite outgrowth of peripheral neurons on immature spinal cord (58) Field of Classi?cation Search substrata,” Neurosci, 1996, 71:773-786. CPC A61K 38/00; A61K 9/0019; A61K 9/0024; A61K 9/5169; C07K 14/78; C07K 2319/735; (Continued) C07K 2/00; B82Y 5/00 See application ?le for complete search history. Primary Examiner * Julie Ha Assistant Examiner * Li Ni Komatsu (56) References Cited (74) Attorney, Agent, or Firm * Casimir Jones, SC. U.S. PATENT DOCUMENTS 2006/0247165 A1 11/2006 Stupp et al. (57) ABSTRACT OTHER PUBLICATIONS The present invention is directed to peptide amphiphile com pounds, compositions and methods of use, wherein nano?ber Cui et al, Spontaneous and X-rayiTriggered Crystallization at Long bundling or epitope aggregation is inhibited. In certain Range in Self-Assembling Filament Networks, Science, 2010, 327, embodiments, the peptide amphiphiles of the present inven pp. SSS-559* tion have increased solubility and reduced nano?ber bun Cui et al, Spontaneous and X-rayiTriggered Crystallization at Long Range in Self-Assembling Filament Networks, Science, 2010, 327, dling. The molecules may be used in pharmaceutical appli supporting materials, pp. 1-47.* cations, for example for in vivo administration to human Angeloni et al, Regeneration of the cavernous nerve by Sonic hedge patients, by increasing biological activity of the compositions hog using aligned peptide amphiphile nano?bers, Biomaterials, toward neurite outgrowth and nerve regeneration. 2011, 32, pp. 1091-1101.* Rudinger, Peptide Hormones, JA Parsons, Ed., 1976, pp. 1-7.* SIGMA, 2004, pp. 1-2.* 5 Claims, 17 Drawing Sheets US 8,748,569 B2 Page 2 (56) References Cited Nakamura et al., “Construction of a multi-functional extracellular matrix protein that increases number of N1E-115 neuroblast cells OTHER PUBLICATIONS having neurites,” J Biomed Mater Res B Appl Biomater, 2009, 91:425-432. Bellamkonda et al., “Laminin oligopeptide derivatized agarose gels Niece et al., “Modi?cation of gelation kinetics in bioactive peptide allow three-dimensional neurite extension in vitro,” J Neurosci Res, amphiphiles,” Biomaterials, 2008, 4501-4509. 1995, 41:501-509. Nomizu et al., “[Identi?cation of biologically active sites in laminin Berat et al., “Peptide-presenting two-dimensional protein matrix on an extracellular matrix protein] ,”Yakugak Zasshi : J Pharm Society supported lipid bilayers: an ef?cient platform for cell adhesion,” Japan, 1998, 118: 566-580, with English Abstract. Biointerphases, 2007, 2: 165-172. Nomizu et a1 ., “Identi?cation of cell binding sites in the laminin alpha Chalazonitis et al., “The alphal subunit of laminin-1 promotes the 1 chain carboxyl-terminal globular domain by systematic screening development of neurons by interacting with LBP110 expressed by of synthetic peptides,” J Biol Chem, 1995, 270: 20583-20590. neural crest-derived cells immuno selected from the fetal mouse gut,” Nomizu et al., “Cell binding sequences in mouse laminin alphal JNeurobiol, 1997, 33: 118-138. chain,” J Biol Chem, 1998, 273: 32491-32499. Chang et al., “Modulation of neural network activity by patterning,” Nomizu et al., “The all-D-con?guration segment containing the Biosens Bioelectron, 2001, 16(7-8): 527-533. IKVAV sequence of laminin A chain has similar activities to the Cornish et al., “Microcontact printing: a versatile technique for the all-L-peptide in vitro and in vivo,” J Biol Chem, 1992, 267: 14118 study of synaptogenic molecules,” Mol Cell Neurosci, 2002, 20: 14121. 140-153. Nomizu et al., “Structure-activity study of a laminin alpha 1 chain Cui et al., “Cerebrum Repair with PHPMA Hydrogel Immobilized active peptide segment Ile-Lys-Val-Ala-Val (IKVAV),” FEBS Lett, with Neurite-Promoting Peptides in Traumatic Brain Injury of Adult 1995, 365: 227-231. Rat Model,” J Bioactive and Compatible Polymers, 2003, 18: 413 Ohga et al., “Design and activity of multifunctional ?brils using 432. receptor-speci?c small peptides,” Biomaterials, 2009, 30: 673 1 -673 8. Duque et al., “Immobilization of biomolecules to plasma polymer Patel et al., “Spatially controlled cell engineering on biodegradable ized penta?uorophenyl methacrylate,” Biomacromolecules, 2010 1 1 : polymer surfaces,” FASEB Journal, 1998, 12: 1447-1454. 2818-2823. Powell et al., “Neural cell response to multiple novel sites on laminin Ehteshami et al., “Immobilization of bioactive peptides on 1,” J Neurosci Res, 2000, 61: 302-312. benzocyclobutene (BCB) surface grafted-dextran for neural implant Ranieri et al., “Spatial control of neuronal cell attachment and dif applications,” Proceedings of the 25th Annual International Confer ferentiation on covalently patterned laminin oligopeptide substrates,” ence IEEE Engineering Med Biol Soc, 2003, 1-4, 25: 2180-2181. Int J DevNeurosci, 1994, 12: 725-735. Heller et al., “Patterned networks of mouse hippocampal neurons on Ranieri et al., “Neuronal cell attachment to ?uorinated ethylene peptide-coated gold surfaces,” Biomaterials, 2005, 26: 883-889. propylene ?lms with covalently immobilized laminin oligopeptides Hynd et al ., “Directed cell growth on protein-functionalized hydro gel YIGSR and IKVAV. II,” J Biomed Mater Res, 1995, 29: 779-785. surfaces,” J Neurosci Methods, 2007, 162: 255-263. Richard et al., “Identi?cation of synthetic peptides derived from Itoh et al., “Development of a nerve scaffold using a tendon chitosan laminin alphal and alpha2 chains with cell type speci?city for neurite tube,” Artif Organs, 2003, 27: 1079-1088. outgrowth,” Exp Cell Res, 1996, 228: 98-105. Jung et al., “Selective and direct immobilization of cysteinyl Saha et al., “Biomimetic interfacial interpenetrating polymer net biomolecules by electrochemical cleavage of azo linkage,” works control neural stem cell behavior,” J Biomed Mater Res A, Langmuir, 2010, 26: 15087-15091. 2007, 81: 240-249. Jung et al., “Co-assembling peptides as de?ned matrices for Saneinejad et al., “Patterned glass surfaces direct cell adhesion and endothelial cells,” Biomaterials, 2009, 30: 2400-2410. process outgrowth of primary neurons of the central nervous system,” Kam et al., “Axonal outgrowth of hippocampal neurons on micro J Biomed Mater Res, 1998, 42:13-19. scale networks of polylysine-conjugated laminin,” Biomaterials, Santiago et al., “Peptide-surface modi?cation of poly(caprolactone) 2001, 22: 1049-1054. with laminin-derived sequences for adipose-derived stem cell appli Kasai et al., “Identi?cation of multiple amyloidogenic sequences in cations,” Biomaterials, 2006, 27: 2962-2969. laminin-1,” Biochemistry, 2007, 46: 3966-3974. Shaw et al., “Toward spinal cord injury repair strategies: peptide Kibbey et al., “A 110-kD nuclear shuttling protein, nucleolin, binds to surface modi?cation of expanded poly (tetra?uoroethylene) ?bers the neurite-promoting IKVAV site of laminin-1,” J Neurosci Res, for guided neurite outgrowth in vitro,” J Craniofacial Surg, 2003, 14: 1995, 42: 314-322.
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